What is he best known for?
The fields of study he is best known for:
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.
His most cited work include:
- A transmembrane helix dimer: structure and implications. (844 citations)
- Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution. (611 citations)
- Order matrix analysis of residual dipolar couplings using singular value decomposition. (443 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Structural genomics (23.24%)
- Stereochemistry (23.24%)
- Crystallography (21.41%)
What were the highlights of his more recent work (between 2007-2021)?
- Structural genomics (23.24%)
- Computational biology (12.79%)
- Stereochemistry (23.24%)
In recent papers he was focusing on the following fields of study:
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.
Between 2007 and 2021, his most popular works were:
- NMR Structure Determination for Larger Proteins Using Backbone-Only Data (223 citations)
- Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?, (143 citations)
- NMR analysis demonstrates immunoglobulin G N-glycans are accessible and dynamic. (136 citations)
In his most recent research, the most cited papers focused on:
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.
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