1997 - Fellow of the American Association for the Advancement of Science (AAAS)
Crystallography, Nuclear magnetic resonance, Protein structure, Nuclear magnetic resonance spectroscopy and Chemical physics are his primary areas of study. The Crystallography study combines topics in areas such as Phospholipid, Lipid bilayer and Ligand. His work in the fields of Nuclear magnetic resonance, such as Helix and Two-dimensional nuclear magnetic resonance spectroscopy, intersects with other areas such as Carbon-13, Electric field and Field.
His Protein structure research is multidisciplinary, incorporating perspectives in Integral membrane protein, Cell biology, Protein folding, Transmembrane domain and Acyl carrier protein. His research integrates issues of Immunoglobulin G, Glycan, Peptide bond, Resonance and Binding site in his study of Nuclear magnetic resonance spectroscopy. The various areas that James H. Prestegard examines in his Chemical physics study include Dipole, Magnetic dipole–dipole interaction, Biomolecule, Molecule and Anisotropy.
James H. Prestegard mostly deals with Structural genomics, Stereochemistry, Crystallography, Nuclear magnetic resonance spectroscopy and Nuclear magnetic resonance. His Structural genomics research includes elements of Genetics, Solution structure and Computational biology. His Stereochemistry study incorporates themes from Sialic acid, Glycosidic bond, Glycolipid, Acyl carrier protein and Chemical shift.
As a part of the same scientific study, James H. Prestegard usually deals with the Crystallography, concentrating on Protein structure and frequently concerns with Residual dipolar coupling. His studies deal with areas such as Proton NMR, Protein secondary structure and Analytical chemistry as well as Nuclear magnetic resonance spectroscopy. His Nuclear magnetic resonance study integrates concerns from other disciplines, such as Chemical physics and Dipole.
James H. Prestegard mainly investigates Structural genomics, Computational biology, Stereochemistry, Biochemistry and Protein structure. The study incorporates disciplines such as Genetics and Solution structure in addition to Structural genomics. His Stereochemistry study combines topics in areas such as Rhodopseudomonas palustris, Acyl carrier protein, Binding site and Chemical shift.
His work carried out in the field of Protein structure brings together such families of science as Crystallography, Protein domain and Cell biology. His Crystallography research is multidisciplinary, incorporating elements of Nuclear magnetic resonance spectroscopy, Residual dipolar coupling, Protein secondary structure, Paramagnetism and Residual. His biological study deals with issues like Amino acid, which deal with fields such as Nuclear magnetic resonance.
His main research concerns Nuclear magnetic resonance spectroscopy, Protein structure, Crystallography, Biochemistry and Binding site. His Nuclear magnetic resonance spectroscopy study focuses on Nuclear magnetic resonance and Stereochemistry. His research in Nuclear magnetic resonance intersects with topics in Dipole, Relaxation, NMR spectra database and Model lipid bilayer.
His work deals with themes such as Cell biology, Protein folding, Biological system, Residual and Membrane lipids, which intersect with Protein structure. The concepts of his Crystallography study are interwoven with issues in Heteronuclear molecule, Paramagnetism, Residual dipolar coupling and Protein secondary structure. His Binding site research focuses on Molecule and how it connects with Ligand.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
Essentials of Glycobiology [Internet]
Ajit Varki;Richard D Cummings;Jeffrey D Esko;Pamela Stanley.
A transmembrane helix dimer: structure and implications.
Kevin R. MacKenzie;James H. Prestegard;Donald M. Engelman.
Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution.
J R Tolman;J M Flanagan;M A Kennedy;J H Prestegard.
Proceedings of the National Academy of Sciences of the United States of America (1995)
Order matrix analysis of residual dipolar couplings using singular value decomposition.
Judit A Losonczi;Michael Andrec;Mark W.F Fischer;James H Prestegard.
Journal of Magnetic Resonance (1999)
NMR structures of biomolecules using field oriented media and residual dipolar couplings.
J. H. Prestegard;H. M. Al-Hashimi;J. R. Tolman.
Quarterly Reviews of Biophysics (2000)
Magnetically-oriented phospholipid micelles as a tool for the study of membrane-associated molecules
Charles R. Sanders;Brian J. Hare;Kathleen P. Howard;James H. Prestegard.
Progress in Nuclear Magnetic Resonance Spectroscopy (1994)
Residual Dipolar Couplings in Structure Determination of Biomolecules
J. H. Prestegard;C. M. Bougault;A. I. Kishore.
Chemical Reviews (2004)
NMR evidence for slow collective motions in cyanometmyoglobin.
J. R. Tolman;John Flanagan;M. A. Kennedy;J. H. Prestegard.
Nature Structural & Molecular Biology (1997)
Structural and Dynamic Analysis of Residual Dipolar Coupling Data for Proteins
Joel R. Tolman;Hashim M. Al-Hashimi;Lewis E. Kay;James H. Prestegard.
Journal of the American Chemical Society (2001)
Domain orientation and dynamics in multidomain proteins from residual dipolar couplings.
Mark W. F. Fischer;Judit A. Losonczi;Jeanne Lim Weaver;James H. Prestegard.
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below: