Alfred_G._Redfield

Alfred G. Redfield

Alfred G. Redfield

American molecular biologist, physicist

Not to be confused with Alfred C. Redfield.

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.

Quick Facts Born, Died ...

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,[4] 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.[5][6][7][8] He published his first article using the phosphorus isotope 31P to probe phospholipids in 2004.[9]

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.[1] In 2007 he was recognized with the Russell Varian Prize for contributing the Redfield Relaxation Theory to the field of nuclear magnetic resonance.[10][11]

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.

Career and research

Early work on NMR resonance saturation in solids and Redfield relaxation theory

Earliest research

Charles P. Slichter wrote that "In 1955, Redfield showed that the conventional theory of saturation did not properly account for the experimental facts of nuclear resonance in solids...[Redfield] showed that the conventional approach essentially defied the second law of thermodynamics.[12]"[13]

Redfield studied NMR with Charles Pence Slichter, assisting with early super conductivity experiments at University of Illinois,[14] Urbana and published the Redfield Theory as a postdoc under Nicolaas Bloembergen at Harvard.[15] At first he studied electron removal in argon, hydrogen and crypton, and the movement of electrons in photo conductors, including his doctoral thesis on the hall effect in diamonds and salt crystals.[16]

After his breakthrough work on relaxation theory, he continued to produce papers on nuclear spin relaxation.[17]

Discovery of the Redfield relaxation theory and equation

Redfield's original article published in the IBM Journal in 1957, and then in the first issue of Advanced Magnetic Resonance in 1965, "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 thermodynamics, 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 streamlined analysis of atomic relationships and explained observations that NMR scientists had not fully theorized. The theory helped explain spin temperature, rotating frame, nuclear spin relaxation, and predicted adiabatic demagnetization and remagnetization in a spin-locked state, and short correlation time.

General spectroscopy

Redfield's interests included discovering techniques to advance the practice of NMR for the purpose of nuclear induction spectroscopy, super conducting magnets, current regulator for inductive loads, practical demonstration and proof of theory, nuclear spin thermodynamics, rare spins in solids, two dimensional NMR efficiencies, computing and data processing, isotope labeling, nuclear Overhauser effect, proteins and their macromolecules in solution, phospholipid approaches. He devised a field cycling device to rapidly move a sample in and out of field that became a precursor to modern fast field cycling instrumentation.

Solid state work

Redfield's NMR career began with work on solids, like metals and superconductors. This work later proved to be useful in the study of the physical and motional relationships between protons in large biological molecules, called macromolecules.

Aqueous state and biochemical work

In 1972, along with Raj V. Gupta, Redfield found a way to cancel out the overwhelming signature spectrum of H2O in biological samples, which allowed the visualization of molecular biological structure in blood cells, nucleic acids, enzymes and phospholipids.[18] [19] He continued to pioneer aqueous techniques using deuterium.[20]

General biochemical work

Redfield continued to develop new techniques to study the structure of protein molecules in solution,[21][22] looking at cancer cells with NMR,[23] the shell of the SARS virus cell[24][25] and at amino acids.[26] Later, using multiple resonances via shuttle and specially prepared samples, he investigated molecular activity in phospholipid vesicles.[27][28][29][30]

Nucleic acids work

Redfield explored the structure and properties of tRNA[31] and related enzymes.

Enzymology and phospholipid membrane work

Redfield explored the function and properties of cell walls.[32][33][34][35][36][37][38][39][40][41][42][43][44][45][46][47]

Shuttle invention

In 2003, Redfield developed a shuttle to move a sample in and out of field rapidly. It was the first to be used on a standard high-field NMR spectrometer.[48]

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."[1]

Early years 1929–1945

  • Redfield was born in Boston, Massachusetts
  • Grew up in Woods Hole, where the Oceanographic Institute employed his father, Alfred C. Redfield.

Harvard and Urbana 1946–1953

  • He graduated from Harvard in 1950 with a B.A., then received his M.S. and Ph.D. degrees in physics from the University of Illinois in 1952 and 1953.[49]

Brandeis 1972–2019

Device to rapidly shuttle a sample in and out of field.
  • In 1972 Redfield joined Brandeis University with a joint appointment in physics and biochemistry.
  • Designed his own spectrometer and apparatus that was the first to specifically target biological systems.
  • The apparatus was similar in design to later commercial units, but because it was housed on shelves it was easy to change out components and calibrate in many ways.
  • The processing software and pulse sequences were original.
  • Pulse sequence was selected by a switch
  • Pulse lengths adjusted with an analog pot for S/N and selective pulse water suppression.
  • He had one physics postdoc and one chemistry or biochemistry postdoc in his lab.
  • National Academy of Sciences member in 1979
  • American Academy of Arts and Sciences Fellow in 1983
  • The Max Delbruck Prize from the American Physical Society in 2006

[50]

Death

Redfield died on July 24, 2019, in Alameda, California.

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.

References

  1. [1]
    Pochapsky, Thomas C. (2020). "Alfred G. Redfield (1929–2019)" (PDF). Biographical Memoirs. National Academy of Sciences.
  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. (eds.). New Methods of Computational Quantum Mechanics. John Wiley & Sons. pp. 77–134. ISBN 978-0-470-14205-9.
  3. [3]
    Patt, Steven L.; Sykes, Brian D. (1972). "Water Eliminated Fourier Transform NMR Spectroscopy". Journal of Chemical Physics. 56 (6): 3182. Bibcode:1972JChPh..56.3182P. doi:10.1063/1.1677669.
  4. [4]
    Bax, A.; Torchia, Dennis A. (2007). "Molecular Machinery in Action". Nature.
  5. [5]
    Brunger, A.T. (1997). "X-ray crystallography and NMR reveal complementary views of structure and dynamics". Nature Structural & Molecular Biology. 4 Suppl: 862–865. PMID 9377160.
  6. [6]
    Hu, Yunfei; Cheng, Kai (2021). "NMR-Based Methods for Protein Analysis". Anal. Chem. 93 (4): 1866–1879. doi:10.1021/acs.analchem.0c03830. PMID 33439619. S2CID 231604522.
  7. [7]
    Farrar, Christian T.; Halkides, Chris; Singel, David J. (1997). "The frozen solution structure of p21 ras determined by ESEEM spectroscopy reveals weak coordination of Thr35 to the active site metal ion". Structure. 5 (8): 1055–1066. doi:10.1016/S0969-2126(97)00257-8. PMID 9309221.
  8. [8]
    Redfield, Alfred G. (1996). Rao, B. D. Nageswara; Kemple, Marvin D (eds.). NMR as a Structural Tool for Macromolecules. Indiana University-Purdue University, Indianapolis (IUPUI) Indianapolis USA: Springer, Boston, MA. pp. 123–132. doi:10.1007/978-1-4613-0387-9. ISBN 978-1-4613-0387-9. S2CID 9936189.
  9. [9]
    Roberts, M.F.; Hedstrom, Lizbeth. (2022). "High Resolution 31P Field Cycling NMR Reveals Unsuspected Features of Enzyme-Substrate-Cofactor Dynamics". Frontiers in Molecular Biosciences. 9: 865519. doi:10.3389/fmolb.2022.865519. PMC 9009223. PMID 35433832.
  10. [10]
    Joynt, R.; Nguyen, Bich Ha; Nguyen, V. (2010). "Theory of decoherence of N-state quantum systems in the Born–Markov approximation". Physics Advances in Natural Sciences: Nanoscience and Nanotechnology. 1 (2): 023001. Bibcode:2010ANSNN...1b3001J. doi:10.1088/2043-6254/1/2/023001. S2CID 135870765.
  11. [11]
    Kuzemsky, A.L. (2006). "Statistical Theory of Spin Relaxation and Diffusion in Solids". Journal of Low Temperature Physics. 143 (5–6): 213–256. arXiv:cond-mat/0512182. Bibcode:2006JLTP..143..213K. doi:10.1007/s10909-006-9219-3. S2CID 54862877.
  12. [12]
    Slichter, Charles P. (1978). Principles of Magnetic Resonance. New York: Springer-Verlag. pp. 188–216. ISBN 3-540-08476-2.
  13. [13]
    Redfield, Alfred G. (1955). "Nuclear Magnetic Resonance Saturation and Rotary Saturation in Solids". Physical Review. 98 (6): 1787–1809. Bibcode:1955PhRv...98.1787R. doi:10.1103/PhysRev.98.1787.
  14. [14]
    Sykora, Stanislav (2008). "The Hebel-Slichter effect". ebyte.it/. S. Sýkora and Extra Byte. Retrieved January 3, 2023. they were helped a lot by Alfred Redfield [10,14,15] who was at that time a promising young NMR relaxation expert at the IBM Laboratories, respected both for his theoretical work [10] and for his experiments (he was already oriented towards variable-field NMR relaxometry).
  15. [15]
    Redfield, Alfred G. (2007). "Alfred G. Redfield Foundations and Structures". In Harris, Robin K; Wasylishen, Roderick L (eds.). Encyclopedia of Magnetic Resonance. West Sussex, England: John Wiley & Sons, Ltd. doi:10.1002/9780470034590. ISBN 978-0471938712.
  16. [16]
    Redfield, Alfred G. (1954). "Electronic Hall effect in diamond". Physical Review. 94 (3): 526–537. Bibcode:1954PhRv...94..526R. doi:10.1103/PhysRev.94.526.
  17. [17]
    Janzen, W.R. (1968). Nuclear magnetic resonance saturation and rapid passage experiments in nonmetalic solids (PhD). University of British Columbia.
  18. [18]
    James, Thomas (December 2, 2012). Nuclear magnetic Resonance in biochemistry. Elsevier. ISBN 978-0323141048.
  19. [19]
    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. Bibcode:1972JPhE....5..437Z. doi:10.1088/0022-3735/5/5/018. PMID 5022523.
  20. [20]
    Lopalco, A.; Douglas, J. (2016). "Determination of pKa and Hydration Constants for a Series of α-Keto-Carboxylic Acids Using Nuclear Magnetic Resonance Spectrometry". J Pharm Sci. 105 (2): 664–672. doi:10.1002/jps.24539. PMC 4703567. PMID 26149194.
  21. [21]
    Pervushin, K.; Riek, R; Wider, G.; Wuthrich, K. (1997). "Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution". Proc Natl Acad Sci U S A. 94 (23): 12366–71. Bibcode:1997PNAS...9412366P. doi:10.1073/pnas.94.23.12366. PMC 24947. PMID 9356455.
  22. [22]
    Gillies, D.G. (1972). "The Application of Fourier Transformation to High Resolution Nuclear Magnetic Resonance Spectroscopy". Annual Reports on NMR Spectroscopy Volume 5. Vol. 5. pp. 557–630. doi:10.1016/S0066-4103(08)60441-X. ISBN 9780125053051.
  23. [23]
    Sharma, Alok K.; Dyba, Marcin (2022). "NMR 1H, 13C, 15N backbone resonance assignments of the T35S and oncogenic T35S/Q61L mutants of human KRAS4b in the active, GppNHp-bound conformation". Biomol NMR Assign. 16 (1): 5045–5052. doi:10.1007/s12104-021-10050-7. PMC 9068649. PMID 34686998. S2CID 239472216.
  24. [24]
    Smith, Albert A.; Bolik-Coulon, Nicolas; Ernst, Matthias; Meier, Beat; Ferrage, Fabian (2021). "How wide is the window opened by high-resolution relaxometry on the internal dynamics of proteins in solution?". Journal of Biomolecular NMR. 75 (2): 119–131. doi:10.1007/s10858-021-00361-1. PMC 8018934. PMID 33759077.
  25. [25]
    Jasenakova, Zuzana; Zapletal, Vojtech; Padrta, Petr; Zachrdla, Milan; Bolik-Coulon, Nicolas; Marquardsen, Thorsten (2020). "Boosting the resolution of low-field 15 N relaxation experiments on intrinsically disordered proteins with triple-resonance NMR" (PDF). Journal of Biomolecular NMR. 74 (2–3): 139–145. doi:10.1007/s10858-019-00298-6. PMID 31960224. S2CID 210841855.
  26. [26]
    Bax, Ad (2011). "Triple resonance three-dimensional protein NMR: Before it became a black box". Journal of Magnetic Resonance. 213 (2): 442–445. Bibcode:2011JMagR.213..442B. doi:10.1016/j.jmr.2011.08.003. PMC 3235243. PMID 21885307.
  27. [27]
    Kurze, V.; Steinbauer, B.; Huber, T. (2000). "A (2)H NMR study of macroscopically aligned bilayer membranes containing interfacial hydroxyl residues". Biophysics Journal. 78 (5): 2441–2451. Bibcode:2000BpJ....78.2441K. doi:10.1016/S0006-3495(00)76788-9. PMC 1300833. PMID 10777740.
  28. [28]
    Roberts, Mary F.; Gershenson, Anne; Reuter, Nathalie (2022). "Phosphatidylcholine Cation—Tyrosine π Complexes: Motifs for Membrane Binding by a Bacterial Phospholipase C". Molecules. 27 (19): 6184. doi:10.3390/molecules27196184. PMC 9572076. PMID 36234717.
  29. [29]
    Smith, Richard D.; Martinovic, Suzana; Anderson, Gordon A.; Pasa-Tolic, Ljiljana; Veenstra, Timothy; Dahlquist, F.W. (1987). "Proteome analysis using selective incorporation of isotopically labeled amino acids". Journal of the American Society for Mass Spectrometry. 11 (1): 78–82. doi:10.1016/S1044-0305(99)00120-8. PMID 10631667. S2CID 11423913.
  30. [30]
    Choi, Yongki; Weiss, Gregory A.; Collins, Philip G. (2008). "Single Molecule Recordings of Lysozyme Activity". Phys Chem Chem Phys. 15 (36): 14879–14895. doi:10.1021/ja710348r. PMC 2893882. PMID 18498165.
  31. [31]
    Fabris, D. (2011). "MS analysis of nucleic acids in the post-genomic era". Anal Chem. 83 (15): 5810–16. doi:10.1021/ac200374y. PMC 3432857. PMID 21651236.
  32. [32]
    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.
  33. [33]
    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.
  34. [34]
    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.
  35. [35]
    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.
  36. [36]
    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.
  37. [37]
    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.
  38. [38]
    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.
  39. [39]
    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.
  40. [40]
    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.
  41. [41]
    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.
  42. [42]
    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.
  43. [43]
    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.
  44. [44]
    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.
  45. [45]
    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.
  46. [46]
    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.
  47. [47]
    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. PMID 32479091.
  48. [48]
    Chou, Ching-Yu (2016). "High Sensitivity High-Resolution Full Range Relaxometry Using a Fast Mechanical Sample Shuttling Device and a Cryo-probe". Journal of Biomolecular NMR. 66 (3): 187–194. doi:10.1007/s10858-016-0066-5. PMID 27744623. S2CID 254656945.
  49. [49]
     This article incorporates text available under the CC BY 4.0 license. https://ismar.org/2019/08/22/alfred-guillou-redfield-1929-2019/
  50. [50]
    "Sad News: Alfred G. Redfield, Emeritus Professor of Physics and Biochemistry".
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