Alfred G. Redfield
| Alfred G. Redfield | |
|---|---|
Alfred G. Redfield in his mid eighties | |
| Born | Alfred Guillou Redfield March 11, 1929.[1] Milton, Massachusetts, U.S. |
| 💀Died | July 24, 2019 Alameda, California, United StatesJuly 24, 2019 |
| 🏫 Education | Harvard College (BA),
University of Illinois, Urbana-Champaign (MS), University of Illinois, Urbana-Champaign (PhD) |
| 💼 Occupation | |
Alfred G. Redfield (March 11, 1929 - July 24, 2019) was an American physicist and biochemist. In 1955 he published the Redfield relaxation theory, effectively moving the practice of NMR or Nuclear magnetic resonance from the realm of classical physics to the realm of semiclassical physics.[2] He continued to find novel magnetic resonance applications to solve real-world problems throughout his life.
Redfield earned degrees at Harvard College (BA 1950, Master’s 1952) and University of Illinois, Urbana-Champaign (Ph.D. 1953). As a post-doc he worked with Nicolaas Bloembergen at Harvard, where he first published the Redfield relaxation theory. IBM Watson Scientific Computing Laboratory hired him in 1955 and he taught at Columbia. While there he published his most important work, the Redfield Relaxation Equation.
In 1971 he published experiments that helped to draw the veil of H2O molecules away from hitherto invisible atoms in large, biological molecules[3] . He continued to innovate specific NMR techniques to view the molecular structure of nucleic acids and enzymes. Beginning in 1996 the NMR Field Cycling community began to realize that slow NMR had an advantage over X-ray crystallography for observing large, biological molecule(macromolecule) dynamics, which can't be captured by high energy NMR or crystallography. In 1996 he released an article exploring field cycling as a way to study macromolecules in more detail[4] . He published his first article using the phosphorous isotope 31P to probe phospholipids in 2004[5] .
He became a fellow of the American Physical Society in 1959 was elected to the National Academy of Sciences in 1979, and named a Fellow of the American Academy of Arts and Sciences (AAAS) in 1983. Redfield received the Max Delbruck Prize from the American Physical Society in 2006. In 2007 he was recognized with the Russell Varian Prize for contributing the Redfield Relaxation Theory to the field of nuclear magnetic resonance.[6]
Redfield is descended from a family of pioneering scientists, including his father, Alfred C. Redfield, his second great-grandfather, William Charles Redfield, and his great-grandfather, the naturalist John Howard Redfield.
The Redfield relaxation theory
The Redfield relaxation theory in equation form:
The Redfield relaxation theory represents a transition in theoretical understanding of applied energy levels in atomic nuclei from a classic model to a quantum model. The classic model of nuclear relaxation posited heat transfer, but at high energy levels the old model could not account for the observed nuclear relaxation. Redfield found that in the quantum model, nuclear relaxation at high energy levels could be accounted for. The theory was at first applied to solid-state substances like metals and super conductors but was eventually applicable to many NMR molecular mapping problems.
The equation and theory have been employed in areas such as condensed phase chemical dynamics, verifying spin-boson theories[7] , photolysis Photodissociation, photolysis, or photodecomposition, photosynthesis [8] [9] [10] , electron transfer reactions [8] [11] , and conical intersections[12]
Essential aspects of the Redfield relaxation theory [2]
• Uses a reduced density matrix to ignore, or put aside, daunting aspects of the molecular and atomic (quantum) laws of motion and thermodynamics.
• Estimates the structure and distances of nuclei in a probabilistic way.
• A practical way to verify theoretical molecular chemistry and biology.
• Allows negative values in the equations of motion to prevent otherwise necessary mathematical gymnastics.
• Obviates superfluous calculation of complex environmental effects that in the effective time scale have a relatively small influence on the nuclear relationships being studied.
• Significant savings in both computer time and memory, particularly as numbers become large.
Controversial aspects of the Redfield relaxation theory[2]
• It allows the use of negative numbers to calculate the laws of thermodynamics and rules of motion.
• It gives an approximate and probabilistic result.
Career and research
Early work on NMR resonance saturation in solids and Redfield relaxation theory
Redfield studied NMR with Charles P. Schlichter at University of Illinois, Urbana and Bloembergen at Harvard..[15] At first he studied electron removal in argon,[16] hydrogen and crypton,[17] and the movement of electrons in photo conductors,[18] including the hall effect in diamonds and salt crystals.[19] [20]
After his breakthrough work on relaxation theory, he continued to produce papers on nuclear spin relaxation.[14] [21] [22] [23] [24][25] [26] [27] [28]
Discovery of the Redfield relaxation theory and equation. [23]
Redfield’s original article published in the IBM Journal in 1957 and then in the first issue of Advanced Magnetic Resonance in 1965 titled The Theory of Relaxation Processes explained observations that molecules excited with RF in a magnetic field did not relax as expected in terms of classical physics, but could be explained in terms of quantum physics, yielding a semi-classic explanation of nuclear spin in metals. The theory continues to be useful not only in NMR, but in optics and computational quantum mechanics as well.
The theory streamlines analysis of atomic relationships by ignoring certain environmental factors, called the rotating frame, and focusing on the molecule being investigated. By setting aside larger but for the moment irrelevant pieces of data, the theory simplified and explained observations that NMR scientists had not fully theorized. The theory explained spin temperature, rotating frame, nuclear spin relaxation, the theory predicted adiabatic demagnetization and remagnetization in a spin-locked state, short correlation time. [15]
General spectroscopy
From time to time, Redfield published articles demonstrating techniques to advance the practice of NMR for the purpose of nuclear induction spectroscopy [21], apparatus innovations[29], super conducting magnets[30] , current regulator for inductive loads [31], practical demonstration and proof of theory [32], nuclear spin thermodynamics [33], rare spins in solids [34] [35], Fourier transform treatments [36] [37] [38] [39], two dimensional NMR efficiencies [40], computing and data processing [41][42], isotope labeling [43] [44] [45] [46], nuclear Overhauser effect [47] [48], proteins and their macromolecules in solution [4] [49] [50] [51], phospholipid approaches [52] [5] [53] [54]. He devised a field cycling device to rapidly move a sample in and out of field [55] that became a precursor to modern fast field cycling instrumentation [56].
Solid state work
Redfield's NMR career began with work on solids and this work proved to be highly useful in detailed study of the physical and motional relationships between protons in large biological molecules. He came up with his Redfield relaxation theory while researching solids like metals and superconductors. [18] [24] [57] [19] [20] [18] [22] [58] [59] [60] [61] [62] [63] [64] [65] [66] [67] [68] [69] [70] [71]
Aqueous state and biochemical work
Redfield found a way to cancel out the overwhelming signature spectrum of H2O in biological samples, which allowed scientists to visualize molecular biological structure in blood cells, nucleic acids, Enzymes and Phospholipids.[3]
James, Thomas (December 2, 2012). Nuclear magnetic Resonance in biochemistry. Elsevier. ISBN 978-0323141048. Search this book on
[72]
[73]
[74]
[75]
[76]
General biochemical work
Turning his attention from the solid state work of the 50s and 60s, Redfield began to look at biological molecules such as the proteins transferrin and cytochrome C in the late 60s and early 70s. By finding a way to see target molecules despite an overwhelming spectral signal from the surrounding aqueous solution, he began to use NMR for biological studies. [77] [78] [79] [80] [81] [82] [83]
In the late seventies he turned his attention to the activity of enzymes at the molecular level by using various methods to 'catch' the enzyme molecules interacting.[84] [85] [86]
In the late 80s and 90s he worked with various collaborators to discover the structure of animal cell proteins, looking for the on/off switch for cell growth and investigating the way large and small proteins migrate through the phospholipid vesicles of cells. People brought their difficult and important bio-molecular structure problems to him and using NMR he helped them see the morphology and kinetics of the molecules. [87][88] [89] [90] [91].
In the 2000s he looked at the shell of the SARS virus cell [92] and at amino acids [93], as well as molecular activity in phospholipid vesicles [94].
1988 to 1990 he explored the structure of larger proteins such as nucleic acids [95] [96] [97] [98].
Around 2008 he turned his attention to the structure of phospholipids [99] [100]
Nucleic acids work
Exploring the structure and Properties of DNA and tRNA[101] [102] [103] [104] [105] [106] [107] [108] [109] [110] [111] [112] [113] [114] [115] [116] [117] [118] [119] [120] [121] [122] [123] [124] [125] [126] [127] [128]
Enzymology & phospholipid membrane work
Exploring the Function and Properties of Cell Walls[129] [130] [131] [132] [133] [134] [135] [136] [137] [138] [139] [140] [141] [142] [143] [144]
Shuttle invention
A Device for Rapidly Moving a Sample In and Out of Field[145]
Biography
"Alfred Redfield was one of the giants of nuclear magnetic resonance (NMR), in terms of both his contributions to fundamental science and the practical application of magnetic resonance to real world problems. As a teenager during World War II, he learned circuitry and electronics that he would later apply to building his own NMR spectrometers. However, his genius was not limited to NMR; Redfield relaxation theory has been applied to statistical mechanical and spectroscopic systems throughout the physical sciences. He was elected to the National Academy of Sciences in 1979 and named a Fellow of the American Academy of Arts and Sciences (AAAS) in 1983. Redfield received the Max Delbrück Prize from the American Physical Society in 2006."
Harvard and Urbana 1945 - 1953
IBM and Columbia 1953 - 1972
Brandeis 1972 - 2019

Alameda, Ca 2015 - 2019
Dr. Alfred G. Redfield Publications:
NAAS obit REFERENCES
NAAS SELECTED BIBLIOGRAPHY
1955 Nuclear magnetic resonance saturation and rotary saturation in solids. Physical Review 98(6):1787–1809.
1959 With A. G. Anderson. Nuclear spin-lattice relaxation in metals. Physical Review 116(3):583–591. 1963. Pure nuclear electric quadrupole resonance in impure copper. Physical Review 130(2):589-595.
1963 With M. Eisenstadt. Nuclear spin relaxation by translational diffusion in solids. Physical Review 132(2):635–643. Pure nuclear electric quadrupole resonance in impure copper. Physical Review 130(2):589–595.
1965 The theory of relaxation processes. In Advances in Magnetic and Optical Resonance, pp. 1–32.
1967 Local-field mapping in mixed-state superconducting vanadium by nuclear magnetic resonance. Physical Review 162(2):367–374.
1969 Nuclear spin thermodynamics in the rotating frame. Science 164(3883):1015-1023.
1970 With R. K. Gupta. Double nuclear magnetic resonance observation of electron exchange between ferri- and ferrocytochrome c. Science 169(3951):1204–1206.
1971 With H. E. Bleich. Higher resolution NMR of rare spins in solids [1]. The Journal of Chemical Physics 55(11):5405–5406.
1971 With R. K. Gupta. Pulsed Fourier transform nuclear magnetic resonance spectrometer. In Advances in Magnetic and Optical Resonance, pp.81–115.
1973 With A. Z. Genack. Nuclear spin diffusion and its thermodynamic quenching in the field gradients of a Type-II superconductor. Physical Review Letters 31(19):1204–1207.
1975 With S. D. Kunz and E. K. Ralph. Dynamic range in Fourier transform proton magnetic resonance. Journal of Magnetic Resonance 19(1):114–117.
1978 With J. D. Stoesz and D. Malinowski. Cross relaxation and spin diffusion effects on the proton NMR of biopolymers in H2 O. Solvent saturation and chemical exchange in superoxide dismutase. FEBS Letters 91(2):320–324. 11 ALFRED REDFIELD
1979 With P. D. Johnston and N. Figueroa. Real-time solvent exchange studies of the imino and amino protons of yeast phenylalanine transfer RNA by Fourier transform NMR. Proceedings of the National Academy of Sciences U.S.A. 76(7):3130–3134.
1983 Stimulated echo NMR spectra and their use for heteronuclear two-dimensional shift correlation. Chemical Physics Letters 96(5):537–540.
1986 With M. A. Weiss and R. H. Griffey. Isotope-detected 1 H NMR studies of proteins: A general strategy for editing interproton nuclear Overhauser effects by heteronuclear decoupling, with application to phage λ repressor. Proceedings of the National Academy of Sciences, U.S.A. 83(5):1325–1329.
1987 With L. P. McIntosh, et al. Proton NMR measurements of bacteriophage T4 lysozyme aided by 15N isotopic labeling: Structural and dynamic studies of larger proteins. Proceedings of the National Academy of Sciences, U.S.A. 84(5):1244–1248.
1989 With S. C. Burk, M. Z. Papastavros, and F. McCormick. Identification of resonances from an oncogenic activating locus of human N-RAS-encoded p21 protein using isotopeedited NMR. Proceedings of the National Academy of Sciences, U.S.A. 86(3):817–820.
2009. With Shi, X. et al. Modulation of Bacillus thuringiensis phosphatidylinositolspecific phospholipase C activity by mutations in the putative dimerization interface. Journal of Biological Chemistry 284(23):15607-15618.
2009 With M. Pu, J. Feng, and M. F. Roberts. Enzymology with a spin-labeled phospholipase C: Soluble substrate binding by 31P NMR from 0.005 to 11.7 T. Biochemistry 48(35):8282–8284. With X. Shi, et al. Modulation of Bacillus thuringiensis phosphatidylinositolspecific phospholipase C activity by mutations in the putative dimerization interface. Journal of Biological Chemistry 284(23):15607–15618.
2016 With M. M. Rosenberg, M. F. Roberts, and L. Hedstrom. Substrate and cofactor dynamics on guanosine monophosphate reductase probed by high resolution field cycling 31P NMR relaxometry. Journal of Biological Chemistry 291(44):22988–22998.
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References
- ↑ www
.nasonline .org /publications /biographical-memoirs /memoir-pdfs /redfield-alfred-g .pdf[bare URL PDF] - ↑ 2.0 2.1 2.2 Pollard, W. Thomas; Felts, Anthony K.; Friesner, Richard A. (September 9, 2009). "The Redfield Equation in Condensed-Phase Quantum Dynamics". In Prigogine, Ilya; Rice, Stuart A. New Methods of Computational Quantum Mechanics. John Wiley & Sons. pp. 77–134. ISBN 978-0-470-14205-9. Search this book on
- ↑ 3.0 3.1 Redfield, Alfred G.; Gupta, R.K. (1971). "Pulsed Fourier-transform NMR spectrometer for use with H2O solutions". Journal of Chemical Physics. 54 (3): 1418–1419. Bibcode:1971JChPh..54.1418R. doi:10.1063/1.1674990.
- ↑ 4.0 4.1 Redfield, Alfred G. (1996). "NMR as a Structural Tool for Macromolecules". In Rao, B. D. Nageswara; Kemple, Marvin D. Field-cycling NMR applied to macromolecular structure and dynamics. Indiana University-Purdue University, Indianapolis (IUPUI) Indianapolis USA: Springer, Boston, MA. p. 123-132. doi:10.1007/978-1-4613-0387-9. ISBN 978-1-4613-0387-9. Unknown parameter
|s2cid=ignored (help) Search this book on
- ↑ 5.0 5.1 Roberts, M.F.; Redfield, Alfred G. (2004). "High-resolution 31P field cycling NMR as a probe of phospholipid dynamics". Journal of American Chemical Society. 126 (42): 13765–1377. doi:10.1021/ja046658k. PMID 15493936.
- ↑ Redfield, A.G. (1957). "On the Theory of Relaxation Processes". IBM Journal of Research and Development. 1: 19–31. doi:10.1147/rd.11.0019.
- ↑ Yang, Chou-Hsun; Wang, Haobin (2020). "Heat Transport in a Spin-Boson Model at Low Temperatures: A Multilayer Multiconfiguration Time-Dependent Hartree Study". Entropy. 22 (10): 1099. Bibcode:2020Entrp..22.1099Y. doi:10.3390/e22101099. PMC 7597201 Check
|pmc=value (help). PMID 33286870 Check|pmid=value (help). - ↑ 8.0 8.1 Ishizaki, Akihito; Fleming, Graham R. (2009). "On the adequacy of the Redfield equation and related approaches to the study of quantum dynamics in electronic energy transfer". Journal of Chemical Physics. 130 (234110): 234110. Bibcode:2009JChPh.130w4110I. doi:10.1063/1.3155214. PMID 19548714.
- ↑ Tao, Ming Jie; Zhang, Na-Na; Wen, Peng-Yu; Deng, Fu-Guo; Ai, Ching; Long, Gui-Lu (2020). "Coherent and incoherent theories for photosynthetic energy transfer". Science Bulletin. 65 (4): 318–328. arXiv:1907.06528. Bibcode:2020SciBu..65..318T. doi:10.1016/j.scib.2019.12.009. Unknown parameter
|s2cid=ignored (help) - ↑ Powell, Daniel D.; Wasielewski, Michael R.; Ratner, Mark A. (2017). "Redfield Treatment of Multipathway Electron Transfer in Artificial Photosynthetic Systems". Journal of Physical Chemistry B. 121 (29): 7190–7203. doi:10.1021/acs.jpcb.7b02748. PMID 28661144.
- ↑ Jean, John M.; Friesner, Richard A.; Fleming, Graham (1992). "Application of a multilevel Redfield theory to electron transfer in condensed phases". J. Chem. Physics. 96 (5827): 5827–5842. Bibcode:1992JChPh..96.5827J. doi:10.1063/1.462858.
- ↑ Kuhl, Axel; Domcke, Wolfgang (2002). "Multilevel Redfield description of the dissipative dynamics at conical intersections". Journal of Chemical Physics. 116 (1): 263–274. doi:10.1063/1.462858.
- ↑ Redfield, Alfred G. (1955). "Nuclear magnetic resonance saturation and rotary saturation in solids". Physics Review. 98 (6): 1787–1809. Bibcode:1955PhRv...98.1787R. doi:10.1103/PhysRev.98.1787.
- ↑ 14.0 14.1 Redfield, Alfred G. (1955). "Nuclear Magnetic Resonance Saturation and Rotary Saturation in Solids". Physics Review. 98 (6): 1787–1809. Bibcode:1955PhRv...98.1787R. doi:10.1103/PhysRev.98.1787.
- ↑ 15.0 15.1 Redfield, Alfred G. (2007). "Alfred G. Redfield Foundations and Structures". In Harris, Robin K; Wasylishen, Roderick L. Encyclopedia of Magnetic Resonance. West Sussex, England: John Wiley & Sons, Ltd. doi:10.1002/9780470034590. ISBN 978-0471938712.[1]
- ↑ Redfield, Alfred G. (1951). "Electron removal in argon afterglows". Physics Review. 82 (6): 874–876. Bibcode:1951PhRv...82..874R. doi:10.1103/PhysRev.82.874.
- ↑ Redfield, Alfred G. (1951). "Electron removal processes in hydrogen, argon, and krypton". Physics Review. 82 (4): 566. doi:10.1103/PhysRev.82.566.
- ↑ 18.0 18.1 18.2 Redfield, Alfred G. (1953). "Electronic Hall effect in NaCl". Physics Review. 91 (3): 753. Bibcode:1953PhRv...91..753R. doi:10.1103/PhysRev.91.753.
- ↑ 19.0 19.1 Redfield, Alfred G. (1954). "Electronic Hall effect in diamond". Physics Review. 94 (3): 526–537. Bibcode:1954PhRv...94..526R. doi:10.1103/PhysRev.94.526.
- ↑ 20.0 20.1 Redfield, Alfred G. (1954). "Electronic Hall effect in the alkali halides". Physics Review. 94 (3): 537–540. Bibcode:1954PhRv...94..537R. doi:10.1103/PhysRev.94.537.
- ↑ 21.0 21.1 Redfield, Alfred G. (1956). "Nuclear induction spectrometer for use at high rf intensities and low temperatures". Review of Scientific Intruments. 27 (4): 230–232. Bibcode:1956RScI...27..230R. doi:10.1063/1.1715528.
- ↑ 22.0 22.1 Redfield, Alfred G. (1956). "Nuclear spin-lattice relaxation time in copper and aluminum". Physics Review. 101 (1): 67–68. Bibcode:1956PhRv..101...67R. doi:10.1103/PhysRev.101.67.
- ↑ 23.0 23.1 Redfield, Alfred G. (1957). "On the theory of relaxation processes". IBM Journal of Research & Development. 1 (1): 19–31. doi:10.1147/rd.11.0019.
- ↑ 24.0 24.1 Redfield, Alfred G. (1953). "Hall mobility in insulation photoconductors". Physics Review. 94 (3): 244. doi:10.1103/PhysRev.94.244 (inactive July 31, 2022). NO EVIDENCE FOR THIS REFERENCE
- ↑ Whitfield, G.; Redfield, Alfred G. (1957). "Paramagnetic resonance detection along the polarizing field direction". Physics Review. 106 (5): 918–920. Bibcode:1957PhRv..106..918W. doi:10.1103/PhysRev.106.918.
- ↑ Redfield, Alfred G. (1959). "Spatial diffusion of spin energy". Physics Review. 116 (2): 315–316. Bibcode:1959PhRv..116..315R. doi:10.1103/PhysRev.116.315.
- ↑ Redfield, Alfred G. (1962). "Statistical theory of spin resonance saturation". Physics Review. 128 (5): 2251–2253. Bibcode:1962PhRv..128.2251R. doi:10.1103/PhysRev.128.2251.
- ↑ Redfield, Alfred G. (1965). "The theory of relaxation processes". Advanced Magnetic Resonance. Advances in Magnetic and Optical Resonance. 1 (1): 1–32. doi:10.1016/B978-1-4832-3114-3.50007-6. ISBN 9781483231143.
- ↑ Redfield, Alfred G.; Moleski, C. (1972). "Vibrating sample magnetometer for protein research". Review of Scientific Instruments. 43 (5): 760–762. Bibcode:1972RScI...43..760R. doi:10.1063/1.1685752.
- ↑ Redfield, Alfred G. (1979). "Nuclear magnetic resonance in biochemistry using superconducting magnets". Journal of Magnetism and Magnetic Materials. 11 (1–3): 197–199. Bibcode:1979JMMM...11..197R. doi:10.1016/0304-8853(79)90264-6.
- ↑ Redfield, Alfred G.; Fite, W.; Bleich, H.E. (1968). "Precision high speed current regulators for occasionally switched inductive loads". Review of Scientific Instrumentation. 39 (5): 710–715. Bibcode:1968RScI...39..710R. doi:10.1063/1.1683481.
- ↑ Redfield, Alfred G. (1991). "On the upper bound of spin polarization transfer". Journal of Magnetic Resonance(1969). 92 (3): 642–644. Bibcode:1991JMagR..92..642R. doi:10.1016/0022-2364(91)90363-X.
- ↑ Redfield, Alfred G. (1969). "Nuclear spin thermodynamics in the rotating frame". Journal of Magnetic Resonance. 164 (3883): 1015–1023. Bibcode:1969Sci...164.1015R. doi:10.1126/science.164.3883.1015. PMID 17796604.
- ↑ Redfield, Alfred G.; Yu, W.N. (1969). "Moment-method calculation of magnetization and interspin-energy diffusion". Physics Review. 177 (2): 1018. Bibcode:1969PhRv..177.1018R. doi:10.1103/PhysRev.177.1018.
- ↑ Bleich, H.E.; Redfield, Alfred G. (1971). "Higher resolution NMR of rare spins in solids". Journal of Chemical Physics. 55 (11): 5405–5406. Bibcode:1971JChPh..55.5405B. doi:10.1063/1.1675686.
- ↑ Redfield, Alfred G.; Kunz, S.D.; Ralph, E.K. (1975). "Dynamic range in Fourier transform proton magnetic resonance". Journal of Magnetic Resonance. 19 (1): 114–117. Bibcode:1975JMagR..19..114R. doi:10.1016/0022-2364(75)90035-9.
- ↑ Redfield, Alfred G.; Kunz, S.D. (1969). "Quadrature Fourier NMR detection: Simple multiplex for dual detection and discussion". Journal of Magnetic Resonance. 19 (2): 250–254. doi:10.1016/0022-2364(75)90073-6.
- ↑ Genack, A.Z.; Redfield, Alfred G. (1975). "Theory of nuclear spin diffusion in a spatially varying magnetic field". Physics Review B. 12 (1): 78–87. Bibcode:1975PhRvB..12...78G. doi:10.1103/PhysRevB.12.78.
- ↑ Waelder, S.; Lee, L.; Redfield, Alfred G. (1975). "Letter: Nuclear magnetic resonance studies of exchangeable protons. I. Fourier transform saturation-recovery and transfer of saturation of the tryptophan indole nitrogen proton". Journal of the American Chemical Society. 97 (10): 2927–2928. doi:10.1021/ja00843a066. PMID 1133343.
- ↑ Redfield, Alfred G. (1983). "Fast and economical treatment of 2D NMR data". Journal of Magnetic Resonance. 52 (2): 310–312. Bibcode:1983JMagR..52..310R. doi:10.1016/0022-2364(83)90201-9.
- ↑ Kunz, S.; Redfield, Alfred G. (1983). "Inexpensive moderate speed input processor and buffer memory for NMR instrumentation". Review of Scientific Instruments. 54 (4): 503–504. Bibcode:1983RScI...54..503K. doi:10.1063/1.1137401.
- ↑ Redfield, Alfred G.; Kunz, S.D.; Ralph, E.K. (1994). "Simple NMR input system using a digital signal processor". Journal of Magnetic Resonance Series A. 108 (2): 234–237. Bibcode:1994JMagR.108..234R. doi:10.1006/jmra.1994.1116.
- ↑ Griffey, R.H.; Redfield, Alfred G. (1985). "Identification of isotope-labeled resonances in two-dimensional proton-proton correlation and exchange spectroscopy with gated heteronuclear decoupling". Journal of Magnetic Resonance. 65 (2): 344–347. Bibcode:1985JMagR..65..344G. doi:10.1016/0022-2364(85)90016-2.
- ↑ Griffey, R.H.; Jarema, M.A.; Kunz, S.; Rosevear, P.R.; Redfield, Alfred G. (1985). "Isotopic-label-directed observation of the nuclear Overhauser effect in poorly resolved proton NMR spectra". Journal of the American Chemical Society. 107 (3): 711–712. doi:10.1021/ja00289a037.
- ↑ Weiss, M.A.; Redfield, Alfred G.; Griffey, R.H. (1986). "Isotope-detected 1H NMR studies of proteins: a general strategy for editing interproton nuclear Overhauser effects by heteronuclear decoupling, with application to phage lambda repressor". Proc. Natl. Acad. Sci. U. S. A. 83 (5): 1325–1329. Bibcode:1986PNAS...83.1325W. doi:10.1073/pnas.83.5.1325. PMC 323068. PMID 3006046.
- ↑ McIntosh, L.P.; Dahlquist, F.W.; Redfield, Alfred G. (1987). "Proton NMR and NOE structural and dynamic studies of larger proteins and nucleic acids aided by isotope labels: T4 lysozyme". Journal of Biomolecular Structure and Dynamics. 5 (1): 21–34. doi:10.1080/07391102.1987.10506372. PMID 3271466.
- ↑ Massefski, W.; Redfield, Alfred G. (1988). "Elimination of multiple-step spin diffusion effects in two-dimensional NOE spectroscopy of nucleic acids". Journal of Magnetic Resonance. 78 (1): 150–155. Bibcode:1988JMagR..78..150M. doi:10.1016/0022-2364(88)90166-7.
- ↑ Lowry, D.F.; Redfield, Alfred G.; McIntosh, L.P.; Dahlquist, F.W. (1988). "One-dimensional nuclear Overhauser effect with two-dimensional heteronuclear multiple quantum coherence detection: Proton-proton nitrogen-15 correlation in T4 lysozyme". Journal of the American Chemical Society. 110 (20): 6885–6886. doi:10.1021/ja00228a048.
- ↑ Redfield, Alfred G.; Kunz, S.D. (1998). "Analog filtering of large solvent signals for improved dynamic range in high-resolution NMR". Journal of Magnetic Resonance. 130 (1): 111–118. Bibcode:1998JMagR.130..111R. doi:10.1006/jmre.1997.1288. PMID 9469905.
- ↑ Ivanov, G.; Redfield, Alfred G. (1998). "Development of a field cycling NMR system for PQR detection in biopolymers". Materials Science/Zeitschrift für Naturforschung A. 53 (6–7): 269–273. Bibcode:1998ZNatA..53..269I. doi:10.1515/zna-1998-6-703. Unknown parameter
|s2cid=ignored (help) - ↑ Ivanov, D.; Redfield, Alfred G. (2004). "Field-cycling method with central transition readout for pure quadrupole resonance detection in dilute systems". Journal of Magnetic Resonance. 166 (1): 19–27. Bibcode:2004JMagR.166...19I. doi:10.1016/j.jmr.2003.10.006. PMID 14675815.
- ↑ Roberts, M.F.; Cui, Q.; Turner, C.J.; Case, D.A.; Redfield, Alfred G. (2004). "High-resolution field-cycling NMR studies of a DNA octamer as a probe of phosphodiester dynamics and comparison with computer simulation". Biochemistry. 43 (12): 3637–3650. doi:10.1021/bi035979q. PMID 15035634.
- ↑ Roberts, M.F.; Redfield, Alfred G. (2004). "Phospholipid bilayer surface configuration probed quantitatively by 31P field-cycling NMR". Proc. Natl. Acad. Sci. U. S. A. 101 (49): 17066–17071. Bibcode:2004PNAS..10117066R. doi:10.1073/pnas.0407565101. PMC 535391. PMID 15569928.
- ↑ Klauda, J.B.; Roberts, M.F.; Redfield, Alfred G.; Brooks, B.R.; Pastor, R.W. (2008). "Rotation of lipids in membranes: molecular dynamics simulation, 31P spin-lattice relaxation, and rigid-body dynamics". Biophysics Journal. 94 (8): 3074–3083. Bibcode:2008BpJ....94.3074K. doi:10.1529/biophysj.107.121806. PMC 2275712. PMID 18192349.
- ↑ Redfield, Alfred G. (2012). "High-resolution NMR field-cycling device for full-range relaxation and structural studies of biopolymers on a shared commercial instrument". Journal of Biomolecular NMR. 52 (2): 159–717. doi:10.1007/s10858-011-9594-1. PMID 22200887. Unknown parameter
|s2cid=ignored (help) - ↑ Anoardo, E.; Galli, G.; Ferrante, G. (2001). "Fast-field-cycling NMR: Applications and instrumentation". Appl. Magn. Reson. 20 (3): 365–404. doi:10.1007/BF03162287. Unknown parameter
|s2cid=ignored (help) - ↑ Redfield, Alfred G. (1954). "An electrodynamic perturbation theorem, with application to nonreciprocal systems". Journal of Applied Physics. 25 (8): 1021–1024. Bibcode:1954JAP....25.1021R. doi:10.1063/1.1721784.
- ↑ Anderson, A.G.; Redfield, Alfred G. (1959). "Nuclear spin-lattice relaxation in metals". Physics Review. 116 (3): 583–591. Bibcode:1959PhRv..116..583A. doi:10.1103/PhysRev.116.583.
- ↑ Redfield, Alfred G. (1959). "Nuclear spin relaxation time in superconducting aluminum". Physics Review Letters. 3 (85): 85–86. Bibcode:1959PhRvL...3...85R. doi:10.1103/PhysRevLett.3.85.
- ↑ Masuda, Y.; Redfield, Alfred G. (1962). "Nuclear spin-lattice relaxation in superconducting aluminum". Physics Review. 125 (1): 159–163. Bibcode:1962PhRv..125..159M. doi:10.1103/PhysRev.125.159.
- ↑ Redfield, Alfred G.; Blume, R.J. (1963). "Nuclear magnetic resonance saturation in lithium". Physics Review. 129 (4): 1545–1548. Bibcode:1963PhRv..129.1545R. doi:10.1103/PhysRev.129.1545.
- ↑ Redfield, Alfred G. (1963). "Pure nuclear electric quadrupole resonance in impure copper". Physics Review. 130 (2): 589–595. Bibcode:1963PhRv..130..589R. doi:10.1103/PhysRev.130.589.
- ↑ Eisenstadt, M.; Redfield, Alfred G. (1963). "Nuclear spin relaxation by translational diffusion in solids". Physics Review. 132 (2): 635–632. Bibcode:1963PhRv..132..635E. doi:10.1103/PhysRev.132.635.
- ↑ Hecht, R.; Redfield, Alfred G. (1963). "Overhauser effect in metallic lithium and sodium". Physics Review. 132 (3): 972–977. Bibcode:1963PhRv..132..972H. doi:10.1103/PhysRev.132.972.
- ↑ Masuda, Y.; Redfield, Alfred G. (1964). "Size effect of nuclear spin-relaxation time in superconducting aluminum". Physics Review. 133 (4A): A944–A947. Bibcode:1964PhRv..133..944M. doi:10.1103/PhysRev.133.A944.
- ↑ Fite, W.; Redfield, Alfred G. (1965). "Superconducting mixed-state-structure determination in vanadium by nuclear magnetic resonance and relaxation". Physics Review. 17 (7): 381–383. doi:10.1103/PhysRevLett.17.381.
- ↑ Fite, W.; Redfield, Alfred G. (1967). "Nuclear spin relaxation in superconducting mixed-state vanadium". Physics Review. 162 (2): 358–367. Bibcode:1967PhRv..162..358F. doi:10.1103/PhysRev.162.358.
- ↑ Redfield, Alfred G. (1967). "Local-field mapping in mixed-state superconducting vanadium by nuclear magnetic resonance". Physics Review. 162 (2): 367–374. Bibcode:1967PhRv..162..367R. doi:10.1103/PhysRev.162.367.
- ↑ Genack, A.Z.; Redfield, Alfred G. (1973). "Nuclear spin diffusion and its thermodynamic quenching in the field gradients of a type-II superconductor". Physics Review of Letters. 31 (19): 1204–1207. Bibcode:1973PhRvL..31.1204G. doi:10.1103/PhysRevLett.31.1204.
- ↑ Bleich, H.E.; Redfield, Alfred G. (1977). "Modified Hartmann-Hahn double NMR in solids for high resolution at low gyromagnetic ratio: CaF2 and quadrupole interaction in MgF2". Journal of Chemical Physics. 67 (11): 5040–5047. Bibcode:1977JChPh..67.5040B. doi:10.1063/1.434727.
- ↑ Redfield, Alfred G. (1983). "Stimulated echo NMR spectra and their use for heteronuclear two-dimensional shift correlation". Chem. Phys. Lett. 96 (5): 537–540. Bibcode:1983CPL....96..537R. doi:10.1016/0009-2614(83)80443-6.
- ↑ Ziessow, D.; Lipsky, S. (1972). "Nuclear magnetic resonance Fourier spectroscopy with pulse and stochastic excitation controlled by an IBM 1800 computer". Journal of Physics E: Scientific Instruments. 5 (5): 437–441. doi:10.1088/0022-3735/5/5/018. PMID 5022523.
- ↑ Redfield, Alfred G.; Waelder, S. (1979). "Water solvent exchange rates of primary amides. Acid-catalyzed NMR saturation transfer as an indicator of rotation and structure of the protonated form". Journal of the American Chemical Society. 101 (21): 6151–6152. doi:10.1021/ja00515a001.
- ↑ Stoesz, J.D.; Malinowski, D.P.; Redfield, Alfred G. (1979). "Nuclear magnetic resonance study of solvent exchange and nuclear Overhauser effect of the histidine protons of bovine superoxide dismutase". Biochemistry. 18 (21): 4669–4675. doi:10.1021/bi00588a030. PMID 40594.
- ↑ Tropp, J.; Redfield, Alfred G. (1980). "Proton magnetic resonance of NADH in water-methanol mixtures. Conformational change and behavior of exchangeable proton resonances as a function of temperature". Journal of the American Chemical Society. 102 (2): 534–538. doi:10.1021/ja00522a016.
- ↑ Griffey, R.H.; Redfield, Alfred G. (1987). "Proton-detected heteronuclear edited and correlated nuclear magnetic resonance and nuclear Overhauser effect in solution". Quarterly Reviews of Biophysics. 19 (1–2): 51–82. doi:10.1017/S0033583500004029. PMID 2819934. Unknown parameter
|s2cid=ignored (help) - ↑ Benz, F.W.; Feeney, J.; Roberts, G.C.K. (1972). "Fourier transform proton NMR spectroscopy in aqueous solution". Journal of Magnetic Resonance. 8 (1): 114–121. doi:10.1016/0022-2364(72)90029-7.
- ↑ Gillies, D.G. (1972). "The Application of Fourier Transformation to High Resolution Nuclear Magnetic Resonance Spectroscopy". Annual Reports on NMR Spectroscopy. 5 (A): 557–630. doi:10.1016/S0066-4103(08)60441-X. ISBN 9780125053051.
- ↑ Aisen, P.; AAsa, R.; Redfield, Alfred G. (1969). "The chromium, manganese, and cobalt complexes of transferrin". Journal of Biological Chemistry. 244 (17): 4628–4633. doi:10.1016/S0021-9258(18)93670-7. PMID 4309148.
- ↑ Gupta, R.K.; Redfield, Alfred G. (1970). "Double nuclear magnetic resonance observation of electron exchange between ferri- and ferrocytochrome c". Science. 169 (3951): 1204–1206. Bibcode:1970Sci...169.1204G. doi:10.1126/science.169.3951.1204. PMID 5450695. Unknown parameter
|s2cid=ignored (help) - ↑ Gupta, R.K.; Redfield, Alfred G. (1970). "NMR double resonance study of azidoferricytochrome c". Biochemical and Biophysical Research Communications. 41 (2): 273–281. doi:10.1016/0006-291x(70)90499-7. PMID 5518158.
- ↑ Gupta, R.K.; Koenig, S.H.; Redfield, Alfred G. (1972). "On the electron transfer between cytochrome c molecules as observed by nuclear magnetic resonance". Journal of Magnetic Resonance. 7 (1): 66–73. Bibcode:1972JMagR...7...66G. doi:10.1016/0022-2364(72)90146-1.
- ↑ Redfield, Alfred G.; Gupta, R.K. (1972). "Pulsed NMR study of the structure of cytochrome c". Cold Spring Harbor Symposia of Quantitative Biology. 36: 405–411. doi:10.1101/SQB.1972.036.01.052. PMID 4343721.
- ↑ Waelder, S.F.; Redfield, Alfred G. (1977). "Nuclear magnetic resonance studies of exchangeable protons. II. The solvent exchange rate of the indole nitrogen proton of tryptophan derivatives". Biopolymers. 16 (3): 623–629. doi:10.1002/bip.1977.360160311. PMID 14742. Unknown parameter
|s2cid=ignored (help) - ↑ Redfield, Alfred G. (1978). "Nuclear magnetic resonance kinetics viewed as enzyme kinetics". Methods in Enzymology. 49: 114–117. doi:10.1016/S0076-6879(78)49018-4. PMID 651673.
- ↑ Stoesz, J.D.; Redfield, Alfred G. (1978). "Cross relaxation and spin diffusion effects on the proton NMR of biopolymers in H2O. Solvent saturation and chemical exchange in superoxide dismutase". FEBS Letters. 91 (2): 320–324. doi:10.1016/0014-5793(78)81201-0. PMID 680139.
- ↑ Burk, S.C.; Papastavros, M.Z.; Roberts, M.F.; Redfield, Alfred G. (1989). "Identification of resonances from an oncogenic activating locus of human N-RAS-encoded p21 protein using isotope-edited NMR". Proc. Natl. Acad. Sci. U. S. A. 86 (3): 817–120. Bibcode:1989PNAS...86..817B. doi:10.1073/pnas.86.3.817. PMC 286568. PMID 2644645.
- ↑ Miller, A.F.; Papastavros, M.Z.; Redfield, Alfred G. (1992). "NMR studies of the conformational change in human N-p21ras produced by replacement of bound GDP with the GTP analog GTP gamma S". Biochemistry. 31 (42): 10208–10216. doi:10.1021/bi00157a007. PMID 1420142.
- ↑ Miller, A.F.; Halkides, C.J.; Redfield, Alfred G. (1993). "An NMR comparison of the changes produced by different guanosine 5'-triphosphate analogs in wild-type and oncogenic mutant p21ras". Biochemistry. 32 (29): 7367–7376. doi:10.1021/bi00080a006. PMID 8338834.
- ↑ Halkides, C.J.; Farrarm, C.T.; Larsen, R.G.; Redfield, Alfred G.; Singel, D.J. (1994). "Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms". Biochemistry. 33 (13): 4019–4035. doi:10.1021/bi00179a031. PMID 8142406.
- ↑ Hu, J.S.; Redfield, Alfred G. (1997). "Conformational and dynamic differences between N-ras P21 bound to GTPgammaS and to GMPPNP as studied by NMR". Biochemistry. 36 (16): 5045–5052. doi:10.1021/bi963010e. PMID 9125526.
- ↑ Clarkson, M.W.; Lei, M.; Eisenmesser, E.Z.; Labeikovsky, W.; Redfield, Alfred G.; Kern, D. (2009). "Mesodynamics in the SARS nucleocapsid measured by NMR field cycling". Journal of Biomolecular NMR. 45 (1–2): 217–225. doi:10.1007/s10858-009-9347-6. PMC 2728245. PMID 19641854.
- ↑ Griffey, R.H.; Redfield, Alfred G.; Loomis, R.E.; Dahlquist, F.W. (1985). "Nuclear magnetic resonance observation and dynamics of specific amide protons in T4 lysozyme cycling relaxometry". Biochemistry. 24 (4): 817–822. doi:10.1021/bi00325a001. PMID 3888265.
- ↑ Ralph, E.K.; Lange, Y.; Redfield, Alfred G. (1985). "Kinetics of proton exchange of phosphatidylethanolamine in phospholipid vesicles". Biophysics Journal. 48 (6): 1053–1057. Bibcode:1985BpJ....48.1053R. doi:10.1016/S0006-3495(85)83868-6. PMC 1329438. PMID 4092067.
- ↑ Griffey, R.H.; Redfield, Alfred G.; McIntosh, L.P.; Oas, T.G.; Dahlquist, F.W. (1986). "Assignment of proton amide resonances of T4 lysozyme by carbon-13 and nitrogen-15 multiple isotopic labeling". Journal of the American Chemical Society. 108 (21): 6816–6817. doi:10.1021/ja00281a066.
- ↑ McIntosh, L.P.; Griffey, R.H.; Muchmore, D.C.; Nielson, C.P.; Redfield, Alfred G.; Dahlquist, F.W. (1987). "Proton NMR measurements of bacteriophage T4 lysozyme aided by 15N isotopic labeling: structural and dynamic studies of larger proteins". Proc. Natl. Acad. Sci. U. S. A. 84 (5): 1244–1248. Bibcode:1987PNAS...84.1244M. doi:10.1073/pnas.84.5.1244. PMC 304403. PMID 3029773.
- ↑ Redfield, Alfred G.; McIntosh, L.P.; Dahlquist, F.W. (1989). "Use of 13C and 15N isotope labels for proton nuclear magnetic resonance and nuclear Overhauser effect. Structural and dynamic studies of larger proteins and nucleic acids". Biological and Medical Experiments Archive/ Archivos de biología y medicina experimentales. 22 (2): 129–137. PMID 2619316.
- ↑ Massefski, W. Jr.; Redfield, Alfred G.; Hare, D.R.; Miller, C. (1990). "Use of 13C and 15N isotope labels for proton nuclear magnetic resonance and nuclear Overhauser effect. Structural and dynamic studies of larger proteins and nucleic acids". Science. 249 (4968): 521–524. doi:10.1126/science.1696395. PMID 1696395.
- ↑ Wang, Y.K.; Chen, W.; Blair, D.; Pu, M.; Xu, Y.; Miller, S.J.; Redfield, Alfred G.; Chiles, T.C.; Roberts, M.F. (2008). "Insights into the structural specificity of the cytotoxicity of 3-deoxyphosphatidylinositols". Journal of the American Chemical Society. 130 (24): 7746–7755. doi:10.1021/ja710348r. PMC 2893882. PMID 18498165.
- ↑ Shi, X.; Shao, C.; Zhang, X.; Zambonelli, C.; Redfield, Alfred G.; Head, J.F.; Seaton, B.A.; Roberts, M.F. (2009). "Modulation of Bacillus thuringiensis phosphatidylinositol-specific phospholipase C activity by mutations in the putative dimerization interface". Journal of Biological Chemistry. 284 (23): 15607–15618. doi:10.1074/jbc.M901601200. PMC 2708857. PMID 19369255.
- ↑ Bell, R.M.; Parsons, S.M.; Dubravac, S.A.; Redfield, Alfred G.; Koshland, D.E. Jr. (1974). "Characterization of slowly interconvertible states of phosphoribosyladenosine triphosphate synthetase dependent on temperature, substrates, and histidine". Journal of Bilogical Chemistry. 249 (13): 4110–4118. doi:10.1016/S0021-9258(19)42490-3. PMID 4368489.
- ↑ Redfield, Alfred G.; Kunz, S.D.; Ralph, E.K. (1975). "Proton magnetic resonance studies of alpha-keto acids". Journal of Biological Chemistry. 250 (2): 527–532. doi:10.1016/S0021-9258(19)41928-5. PMID 234430.
- ↑ Lange, Y.; Ralph, E.K.; Redfield, Alfred G. (1975). "Observation of the phosphatidylethanolamine amino proton magnetic resonance in phospholipid vesicles: inside/outside ratios and proton transport". Biochemical and Biophysical Research Communications. 62 (4): 891–894. doi:10.1016/0006-291x(75)90406-4. PMID 1168058.
- ↑ Huang, T.H.; Redfield, Alfred G. (1976). "NMR study of relative oxygen binding to the alpha and beta subunits of human adult hemoglobin". Journal of Biological Chemistry. 251 (22): 7114–7119. doi:10.1016/S0021-9258(17)32949-6. PMID 993207.
- ↑ Johnston, P.D.; Redfield, Alfred G. (1977). "An NMR study of the exchange rates for protons involved in the secondary and tertiary structure of yeast tRNA Phe". Nucleic Acids Research. 4 (10): 3599–3615. doi:10.1093/nar/4.10.3599. PMC 342676. PMID 337239.
- ↑ Redfield, Alfred G. (1978). "Proton nuclear magnetic resonance in aqueous solutions". Methods in Enzymology. 49: 253–270. doi:10.1016/S0076-6879(78)49014-7. PMID 651668.
- ↑ Johnston, P.D.; Redfield, Alfred G. (1978). "Pulsed FT-NMR double resonance studies of yeast tRNAPhe: specific nuclear Overhauser effects and reinterpretation of low temperature relaxation data". Nucleic Acids Research. 5 (10): 3913–3927. doi:10.1093/nar/5.10.3913. PMC 342719. PMID 364421.
- ↑ Johnston, P.D.; Figueroa, N.; Redfield, Alfred G. (1979). "Real-time solvent exchange studies of the imino and amino protons of yeast phenylalanine transfer RNA by Fourier transform NMR". Proceedings of the National Academy of Sciences, U.S.A. 76 (7): 3130–3134. Bibcode:1979PNAS...76.3130J. doi:10.1073/pnas.76.7.3130. PMC 383777. PMID 386331.
- ↑ Schimmel, P.R.; Redfield, Alfred G. (1980). "Transfer RNA in solution: selected topics". Annual Review of Biophysics & Bioengineering. 9: 181–221. doi:10.1016/0022-2364(75)90035-9. PMID 6994589.
- ↑ Sanchez, V.; Redfield, Alfred G.; Johnston, P.D.; Tropp, J. (1980). "Nuclear Overhauser effect in specifically deuterated macromolecules: NMR assay for unusual base pairing in transfer RNA". Proc. Natl. Acad. Sci. U. S. A. 77 (10): 5659–5662. Bibcode:1980PNAS...77.5659S. doi:10.1073/pnas.77.10.5659. PMC 350128. PMID 7003592.
- ↑ Johnston, P.D.; Redfield, Alfred G. (1981). "Nuclear magnetic resonance and nuclear Overhauser effect study of yeast phenylalanine transfer ribonucleic acid imino protons". Biochemistry. 20 (5): 1147–1156. doi:10.1021/bi00508a016. PMID 7013786.
- ↑ Tropp, J.; Redfield, Alfred G. (1981). "Environment of ribothymidine in transfer ribonucleic acid studied by means of nuclear Overhauser effect". Biochemistry. 8 (25): 2133–2140. doi:10.1021/bi00511a010. PMID 7016173.
- ↑ Johnston, P.D.; Redfield, Alfred G. (1981). "Study of transfer ribonucleic acid unfolding by dynamic nuclear magnetic resonance". Biochemistry. 20 (14): 3996–4006. doi:10.1021/bi00517a008. PMID 7025889.
- ↑ Roy, S.; Redfield, Alfred G. (1981). "Nuclear Overhauser effect study and assignment of D stem and reverse-Hoogsteen base pair proton resonances in yeast tRNAAsp". Nucleic Acids Research. 9 (24): 7073–7083. doi:10.1093/nar/9.24.7073. PMC 327663. PMID 6278454.
- ↑ Roy, S.; Papastavros, M.Z.; Redfield, Alfred G. (1982). "Nuclear Overhauser effect study of yeast aspartate transfer ribonucleic acid". Biochemistry. 21 (24): 6081–6088. doi:10.1021/bi00267a009. PMID 6758844.
- ↑ Schejter, E.; Sanchez, V.; Redfield, Alfred G. (1982). "Nuclear Overhauser effect study of yeast tRNAVal 1: evidence for uridine-pseudouridine base pairing". Nucleic Acids Research. 10 (24): 8297–8305. doi:10.1093/nar/10.24.8297. PMC 327086. PMID 6761651.
- ↑ Roy, S.; Papastavros, M.Z.; Redfield, Alfred G. (1982). "Procedure for C2 deuteration of nucleic acids and determination of A psi 31 pseudouridine conformation by nuclear Overhauser effect in yeast tRNAPhe". Nucleic Acids Research. 10 (24): 8341–8349. doi:10.1093/nar/10.24.8341. PMC 327090. PMID 6761652.
- ↑ Roy, S.; Redfield, Alfred G. (1983). "Assignment of imino proton spectra of yeast phenylalanine transfer ribonucleic acid". Biochemistry. 22 (6): 1386–1390. doi:10.1021/bi00275a010. PMID 6301547.
- ↑ Tropp, J.S.; Redfield, Alfred G. (1983). "Proton exchange rates in transfer RNA as a function of spermidine and magnesium". Nucleic Acids Research. 11 (7): 2121–2134. doi:10.1093/nar/11.7.2121. PMC 325866. PMID 6340067.
- ↑ Roy, S.; Papastavros, M.Z.; Sanchez, V.; Redfield, Alfred G. (1984). "Nitrogen-15-labeled yeast tRNAPhe: double and two-dimensional heteronuclear NMR of guanosine and uracil ring NH groups". Biochemistry. 23 (19): 4395–4400. doi:10.1021/bi00314a024. PMID 6567469.
- ↑ Choi, B.S.; Redfield, Alfred G. (1985). "Nuclear magnetic resonance observation of the triple interaction between A9 and AU12 in yeast tRNAPhe". Nucleic Acids Research. 13 (14): 5249–5254. doi:10.1093/nar/13.14.5249. PMC 321862. PMID 3848815.
- ↑ Choi, B.S.; Redfield, Alfred G. (1986). "NMR study of isoleucine transfer RNA from Thermus thermophilus". Biochemistry. 25 (7): 1529–1534. doi:10.1021/bi00355a010. PMID 3635410.
- ↑ Hall, K.B.; Green, M.R.; Redfield, Alfred G. (1988). "Structure of a pre-mRNA branch point/3' splice site region". Proc. Natl. Acad. Sci. U. S. A. 85 (3): 704–708. Bibcode:1988PNAS...85..704H. doi:10.1073/pnas.85.3.704. PMC 279623. PMID 3422452.
- ↑ Hall, K.B.; Sampson, J.R.; Uhlenbeck, O.C.; Redfield, Alfred G. (1989). "Structure of an unmodified tRNA molecule". Biochemistry. 28 (14): 5794–5801. doi:10.1021/bi00440a014. PMID 2775736.
- ↑ Redfield, Alfred G.; Papastavros, M.Z. (1990). "NMR study of the phosphoryl binding loop in purine nucleotide proteins: evidence for strong hydrogen bonding in human N-ras p21". Biochemistry. 29 (14): 3509–3514. doi:10.1021/bi00466a013. PMID 2191717.
- ↑ Massefski, W. Jr.; Redfield, Alfred G.; Das Sarma, U.; Bannerji, A. (1990). "[7-15N]guanosine-labeled oligonucleotides as nuclear magnetic resonance probes for protein-nucleic acid interaction in the major groove". Journal of the American Chemical Society. 112 (13): 5350–5351. doi:10.1021/ja00169a052.
- ↑ Choi, B.S.; Redfield, Alfred G. (1995). "Proton exchange and basepair kinetics of yeast tRNA(Phe) and tRNA(Asp1)". Journal of Biochemistry. 117 (3): 515–520. doi:10.1093/oxfordjournals.jbchem.a124738. PMID 7629016.
- ↑ Halkides, C.J.; Redfield, Alfred G. (1995). "The effect of 17O on the relaxation of an amide proton within a hydrogen bond". Journal of Biomolecular NMR. 5 (4): 362–366. doi:10.1007/BF00182279. PMID 7647555. Unknown parameter
|s2cid=ignored (help) - ↑ McIntosh, L.P.; Wand, A.J.; Lowry, D.F.; Redfield, Alfred G. (1990). "Assignment of the backbone 1H and 15N NMR resonances of bacteriophage T4 lysozyme". Biochemistry. 29 (27): 6341–6362. doi:10.1021/bi00479a003. PMID 2207079.
- ↑ Lowry, D.F.; Cool, R.H.; Redfield, Alfred G.; Parmeggiani, A. (1991). "NMR study of the phosphate-binding elements of Escherichia coli elongation factor Tu catalytic domain". Biochemistry. 30 (45): 10872–10877. doi:10.1021/bi00109a010. PMID 1932010.
- ↑ Lowry, D.F.; Ahmadian, M.R.; Redfield, Alfred G.; Sprinzl, M. (1992). "NMR study of the phosphate-binding loops of Thermus thermophilus elongation factor Tu". Biochemistry. 31 (11): 2977–2982. doi:10.1021/bi00126a019. PMID 1550823.
- ↑ Choi, B.S.; Redfield, Alfred G. (1992). "NMR study of nitrogen-15-labeled Escherichia coli valine transfer RNA". Biochemistry. 31 (51): 12799–12802. doi:10.1021/bi00166a013. PMID 1463750.
- ↑ Hu, J.S.; Redfield, Alfred G. (1993). "Mapping the nucleotide-dependent conformational change of human N-ras p21 in solution by heteronuclear-edited proton-observed NMR methods". Biochemistry. 32 (26): 6763–6772. doi:10.1021/bi00077a031. PMID 8329399.
- ↑ Ivanov, D.; Bachovchin, W.W.; Redfield, Alfred G. (2002). "Boron-11 pure quadrupole resonance investigation of peptide boronic acid inhibitors bound to alpha-lytic protease". Biochemistry. 41 (5): 1587–1590. doi:10.1021/bi011783j. PMID 11814352.
- ↑ Sivanandam, V.N.; Cai, J.; Redfield, Alfred G.; Roberts, M.F. (2009). "Phosphatidylcholine "wobble" in vesicles assessed by high-resolution 13C field cycling NMR spectroscopy". Journal of the American Chemical Society. 131 (10): 3420–3421. doi:10.1021/ja808431h. PMC 2753464. PMID 19243091.
- ↑ Pu, M.; Fang, X.; Redfield, Alfred G.; Gershenson, A.; Roberts, M.F. (2009). "Correlation of vesicle binding and phospholipid dynamics with phospholipase C activity: insights into phosphatidylcholine activation and surface dilution inhibition". Journal of Biological Chemistry. 284 (24): 16099–16107. doi:10.1074/jbc.M809600200. PMC 2713506. PMID 19336401.
- ↑ Roberts, M.F.; Redfield, Alfred G.; Mohanty, U. (2009). "Phospholipid reorientation at the lipid/water interface measured by high resolution 31P field cycling NMR spectroscopy". Journal of Magnetic Resonance. 97 (1): 132–141. Bibcode:2009BpJ....97..132R. doi:10.1016/j.bpj.2009.03.057. PMC 2711354. PMID 19580751.
- ↑ Pu, M.; Feng, J.; Redfield, Alfred G.; Roberts, M.F. (2009). "Enzymology with a spin-labeled phospholipase C: soluble substrate binding by 31P NMR from 0.005 to 11.7 T". Biochemistry. 48 (35): 8282–8284. doi:10.1021/bi901190j. PMC 2794430. PMID 19663462.
- ↑ Pu, M.; Orr, A.; Redfield, Alfred G.; Roberts, Mary. (2010). "Defining specific lipid binding sites for a peripheral membrane protein in situ using subtesla field-cycling NMR". Journal of Biological Chemistry. 285 (35): 26916–26922. doi:10.1074/jbc.M110.123083. PMC 2930691. PMID 20576615.
- ↑ Gradziel, C.S.; Wang, Y.; Stec, B.; Redfield, Alfred G.; Roberts, M.F. (2014). "Cytotoxic amphiphiles and phosphoinositides bind to two discrete sites on the Akt1 PH domain". Biochemistry. 53 (35): 462–472. doi:10.1021/bi401720v. PMID 24383815.
- ↑ Wei, Y.; Stec, B.; Redfield, Alfred G.; Weerapana, E.; Roberts, M.F. (2015). "Phospholipid-binding sites of phosphatase and tensin homolog (PTEN): exploring the mechanism of phosphatidylinositol 4,5-bisphosphate activation". Journal of Biological Chemistry. 290 (3): 1592–1606. doi:10.1074/jbc.M114.588590. PMC 4340405. PMID 25429968.
- ↑ Rosenberg, M.M.; Redfield, Alfred G.; Roberts, M.F. (2016). "Substrate and cofactor dynamics on guanosine monophosphate reductase probed by high resolution field cycling 31P NMR relaxometry". Journal of Biological Chemistry. 291 (44): 22988–22998. doi:10.1074/jbc.M116.739516. PMC 5087720. PMID 27613871.
- ↑ Rosenberg, M.M.; Redfield, Alfred G.; Roberts, M.F.; Hedstrom, L. (2018). "Dynamic characteristics of guanosine-5'-monophosphate reductase complexes revealed by high-resolution 31P field-cycling NMR relaxometry". Biochemistry. 57 (22): 3146–3154. doi:10.1021/acs.biochem.8b00142. PMC 6467290. PMID 29547266.
- ↑ Rosenberg, M.M.; Yao, T.; Patton, C.G.; Redfield, Alfred G.; Roberts, M.F.; Hedstrom, L. (2020). "Enzyme-substrate-cofactor dynamical networks revealed by high-resolution field cycling relaxometry". Biochemistry. 59 (25): 2359–2370. doi:10.1021/acs.biochem.0c00212. PMC 8364753 Check
|pmc=value (help). PMID 32479091 Check|pmid=value (help). - ↑ Redfield, Alfred G. (2003). "Shuttling device for high-resolution measurements of relaxation and related phenomena in solution at low field, using a shared commercial 500 MHz NMR instrument". Magnetic Resonance in Chemistry. 41 (10): 1587–90. doi:10.1002/mrc.1264. Unknown parameter
|s2cid=ignored (help)
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