Robert G. Bryant

Education

  • AB, Colgate University
  • PhD, Stanford University

Contact

Research Interest(s)

Nuclear Magnetic Resonance in Chemistry and Biophysics

Research Description

Nuclear Magnetic Resonance in Chemistry

Research in the Bryant laboratory employs magnetic resonance methods to study a wide range of molecular dynamics. A primary focus derives from unique instrumentation that permits study of the magnetic field dependence of nuclear spin-lattice relaxation rates. This experimental approach provides an accurate means for characterizing specific intra- and inter-molecular motions over the time range from 1 ms to 0.5 ps. Major efforts include characterizing internal hinge motions in proteins, measuring localized diffusion constants for critical solutes diffusing in the vicinity of unique sites in membranes, and measuring the frequencies of critical side chain motions in protein active sites.

In related work we exploit the effects of a freely diffusing paramagnetic small molecule to characterize the details of how one molecule contacts and explores another. In the protein case, the structural resolution is provided by the 2-dimensional NMR spectral assignments and we may investigate the nature of the intermolecular contacts with the protein as a function of size and charge which permits study of the fundamental aspects of the protein surface energetics that are crucial for molecular recognition processes. An applied and very practical aspect of these experiments is the design and delivery of magnetic contrast agents for applications in clinical magnetic resonance imaging protocols as well as the characterization of liquids in microporous materials.

We also utilize the pressure dependence of amide hydrogen exchange reactions with deuterium oxide to characterize rare structural fluctuations in proteins in a structurally resolved way. Again, we exploit multidimensional NMR spectroscopy to provide the kinetic information at each amide proton position in the folded protein structure. We are primarily exploring how the exchange events are a function of the protein stability and how these pressure measurements provide insights to the structural fluctuations that provide proteins with their catalytic effectiveness.

Selected Publications

  • Goddard Y, Korb J, Bryant R. Nuclear magnetic relaxation dispersion study of the dynamics in solid homopolypeptides. Biopolymers. 2007;86(2): 148-54. PMID: 17345629
  • Lisitza N, Bryant R. Picosecond water dynamics adjacent to charged paramagnetic ions measured by magnetic relaxation dispersion. The Journal of chemical physics. 2007;126(10): 101102. PMID: 17362054
  • Goddard Y, Korb J, Bryant R. Structural and dynamical examination of the low-temperature glass transition in serum albumin. Biophysical journal. 2006;91(10): 3841-7. PMID: 16935952 | PMCID: PMC1630461
  • Teng C, Bryant R. Spin relaxation measurements of electrostatic bias in intermolecular exploration. Journal of magnetic resonance (San Diego, Calif. : 1997). 2006;179(2): 199-205. PMID: 16386442
  • Bryant R, Korb J. Nuclear magnetic resonance and spin relaxation in biological systems. Magnetic resonance imaging. 2005;23(2): 167-73. PMID: 15833608
  • Diakova G, Fuller Z, Victor K, Fumino K, Bryant R. Chromium(III) complexes as intermolecular probes. Journal of magnetic resonance (San Diego, Calif. : 1997). 2005;175(1): 65-72. PMID: 15949749
  • Korb J, Bryant R. Noise and functional protein dynamics. Biophysical journal. 2005;89(4): 2685-92. PMID: 16040739 | PMCID: PMC1366769
  • Teng C, Bryant R. Mapping oxygen accessibility to ribonuclease a using high-resolution NMR relaxation spectroscopy. Biophysical journal. 2004;86(3): 1713-25. PMID: 14990499 | PMCID: PMC1304007
  • Van-Quynh A, Willson S, Bryant R. Protein reorientation and bound water molecules measured by 1H magnetic spin-lattice relaxation. Biophysical journal. 2003;84(1): 558-63. PMID: 12524308 | PMCID: PMC1302636
  • Wagner S, Nevzorov A, Freed J, Bryant R. End-to-end correlation for a C-12 hydrocarbon chain. Journal of magnetic resonance (San Diego, Calif. : 1997). 2003;160(2): 161-5. PMID: 12615159
  • Hern├índez G, Teng C, Bryant R, LeMaster D. O2 penetration and proton burial depth in proteins: applicability to fold family recognition. Journal of the American Chemical Society. 2002;124(16): 4463-72. PMID: 11960476
  • Korb J, Bryant R. Magnetic field dependence of proton spin-lattice relaxation times. Magnetic resonance in medicine : official journal of the Society of Magnetic Resonance in Medicine / Society of Magnetic Resonance in Medicine. 2002;48(1): 21-6. PMID: 12111928
  • Godefroy S, Korb J, Fleury M, Bryant R. New ways of probing surface nuclear relaxation and microdynamics of water and oil in porous media. Magnetic resonance imaging. 2001;19(3): 517-9. PMID: 11445345