2016 - Fellow of the American Academy of Arts and Sciences
Member of the Association of American Physicians
His primary areas of investigation include Stereochemistry, Protein structure, Active site, Bioinformatics and Molecular replacement. The various areas that he examines in his Stereochemistry study include Antiparallel, Protein subunit, Crystal structure, Subtilisin and Catalysis. His Protein structure research focuses on subjects like Binding site, which are linked to Peptide sequence, Protein–protein interaction and Structural biology.
The study incorporates disciplines such as Function, Gene, Protein Data Bank, Protein Data Bank and Structural genomics in addition to Bioinformatics. His Protein Data Bank research is multidisciplinary, relying on both World Wide Web, Database and Structural bioinformatics. His Structural bioinformatics research is multidisciplinary, incorporating elements of Protein structure database, RasMol, Structural alignment and Structure validation.
His scientific interests lie mostly in Stereochemistry, Crystallography, Biochemistry, Protein structure and Crystal structure. His study in Stereochemistry is interdisciplinary in nature, drawing from both Molecule, Hydrogen bond, Binding site and Active site. He usually deals with Crystallography and limits it to topics linked to Crystallization and Biological macromolecule, Macromolecule and Crystal growth.
His research investigates the connection between Biological macromolecule and topics such as Database that intersect with issues in Protein Data Bank. His research investigates the link between Protein structure and topics such as Peptide sequence that cross with problems in Antibody. His biological study deals with issues like Computational biology, which deal with fields such as Bioinformatics.
The scientist’s investigation covers issues in Stereochemistry, Antibody, Biochemistry, Computational biology and Structural genomics. His Stereochemistry research is multidisciplinary, incorporating perspectives in Dimer and Cleavage. His Antibody study deals with Antigen intersecting with Immune system, Phage display and Crystallization.
His research investigates the connection with Computational biology and areas like Function which intersect with concerns in Isomerization, Peptide bond, Protein Data Bank, Wild type and Mutant. His Protein structure study integrates concerns from other disciplines, such as Protein engineering and Peptide. His work is dedicated to discovering how Peptide, Double mutant are connected with Crystallography and other disciplines.
His main research concerns Stereochemistry, Binding site, Biochemistry, Antigen and Immunoglobulin structure. His work carried out in the field of Stereochemistry brings together such families of science as Molecular biology, Cleavage and Fibrinogen. The various areas that Gary L. Gilliland examines in his Binding site study include Amino acid, Protein aggregation, Isoelectric focusing, Peptide sequence and Structural genomics.
His work is connected to Regulatory site, Periplasmic space, Protein structure and Protein engineering, as a part of Biochemistry. His research integrates issues of Crystal growth, Crystallization, Nucleation and Antibody, Phage display in his study of Antigen. He integrates Surface plasmon resonance with Active site in his study.
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The Protein Data Bank
Helen M. Berman;John D. Westbrook;Zukang Feng;Gary Gilliland.
Nucleic Acids Research (2000)
The Protein Data Bank.
Helen M. Berman;Tammy Battistuz;T. N. Bhat;Wolfgang F. Bluhm.
Acta Crystallographica Section D-biological Crystallography (2002)
The Protein Data Bank, 1999–
H. M. Berman;J. Westbrook;Z. Feng;G. L. Gilliland.
International Tables for Crystallography (2006)
The Protein Data Bank and the challenge of structural genomics
Helen M. Berman;T. N. Bhat;Philip E. Bourne;Zukang Feng.
Nature Structural & Molecular Biology (2000)
Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.
I. Sinning;G. J. Kleywegt;S. W. Cowan;P. Reinemer.
Journal of Molecular Biology (1993)
The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution.
Xinhua Ji;Pinghui Zhang;Richard N. Armstrong;Gary L. Gilliland.
Two crystal structures of the B1 immunoglobulin-binding domain of streptococcal protein G and comparison with NMR.
Travis Gallagher;Patrick Alexander;Philip Bryan;Gary L. Gilliland.
Structure of phosphate-free ribonuclease A refined at 1.26 A.
A Wlodawer;L.A Svensson;L Sjolin;G.L. Gilliland.
The Protein Data Bank: unifying the archive
John Westbrook;Zukang Feng;Shri Jain;T. N. Bhat.
Nucleic Acids Research (2002)
Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods.
Xinhua Ji;E. C. Van Rosenvinge;W. W. Johnson;S. I. Tomarev.
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