2014 - Member of the National Academy of Sciences
2014 - Fellow, National Academy of Inventors
2010 - Fellow of the American Academy of Arts and Sciences
2005 - Fellow of the American Association for the Advancement of Science (AAAS)
1993 - Fellow of Alfred P. Sloan Foundation
His primary scientific interests are in Stereochemistry, Peptide, Biochemistry, Protein secondary structure and Foldamer. His studies in Stereochemistry integrate themes in fields like Crystallography, Helix, Folding, Hydrogen bond and Protein structure. Samuel H. Gellman interconnects Antiparallel and Beta sheet in the investigation of issues within Crystallography.
His work deals with themes such as Structure–activity relationship and Protein folding, which intersect with Protein structure. His research on Peptide also deals with topics like
Samuel H. Gellman mainly investigates Stereochemistry, Peptide, Crystallography, Biochemistry and Hydrogen bond. His Stereochemistry study also includes fields such as
His Crystallography research is multidisciplinary, incorporating perspectives in Folding, Antiparallel, Infrared spectroscopy and Amide. His study looks at the relationship between Biochemistry and fields such as Biophysics, as well as how they intersect with chemical problems. His studies deal with areas such as Nuclear magnetic resonance spectroscopy and Intramolecular force as well as Hydrogen bond.
Samuel H. Gellman spends much of his time researching Stereochemistry, Peptide, Biochemistry, Side chain and Amino acid. His Stereochemistry research is multidisciplinary, relying on both Amino acid residue, Protein secondary structure, Residue, Helix and Hydrogen bond. His work is dedicated to discovering how Protein secondary structure, Crystallography are connected with Dimer and other disciplines.
His study in Peptide is interdisciplinary in nature, drawing from both Agonist, Proteolysis, Peptide sequence and Cell biology, Protein–protein interaction. His biological study deals with issues like Biophysics, which deal with fields such as Function. His Side chain research incorporates elements of Protein subunit, Molecule and Structure–activity relationship.
His scientific interests lie mostly in Biochemistry, Stereochemistry, Peptide, Residue and Protein secondary structure. As part of the same scientific family, he usually focuses on Biochemistry, concentrating on Biophysics and intersecting with Membrane, Periplasmic space, Escherichia coli, Lysis and Bacterial outer membrane. His biological study focuses on Foldamer.
Samuel H. Gellman usually deals with Foldamer and limits it to topics linked to Hydrogen bond and Two-dimensional nuclear magnetic resonance spectroscopy and Aqueous solution. As a part of the same scientific family, Samuel H. Gellman mostly works in the field of Peptide, focusing on Peptide sequence and, on occasion, Protein structure. The various areas that Samuel H. Gellman examines in his Protein secondary structure study include Crystallography and Beta sheet.
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Crystal structure of the β2 adrenergic receptor-Gs protein complex.
Søren G. F. Rasmussen;Brian T. DeVree;Yaozhong Zou;Andrew C. Kruse.
Nature (2011)
Foldamers: A Manifesto
Samuel H. Gellman.
Accounts of Chemical Research (1998)
beta-Peptides: from structure to function.
Richard P. Cheng;Samuel H. Gellman;William F. DeGrado.
Chemical Reviews (2001)
Structure of a nanobody-stabilized active state of the β2 adrenoceptor
Søren G F Rasmussen;Hee Jung Choi;Juan Jose Fung;Els Pardon.
Nature (2011)
β-Peptide Foldamers: Robust Helix Formation in a New Family of β-Amino Acid Oligomers
Daniel H. Appella;Laurie A. Christianson;Isabella L. Karle;and Douglas R. Powell.
Journal of the American Chemical Society (1996)
Structure and function of an irreversible agonist-β2 adrenoceptor complex
Daniel M. Rosenbaum;Cheng Zhang;Joseph A. Lyons;Joseph A. Lyons;Ralph Holl.
Nature (2011)
Non-haemolytic β-amino-acid oligomers
Emilie A. Porter;Xifang Wang;Hee-Seung Lee;Bernard Weisblum.
Nature (2000)
Residue-based control of helix shape in beta-peptide oligomers.
Daniel H. Appella;Laurie A. Christianson;Daniel A. Klein;Douglas R. Powell.
Nature (1997)
Foldamers with Heterogeneous Backbones
W. Seth Horne;Samuel H. Gellman.
Accounts of Chemical Research (2008)
Conformation-directing effects of a single intramolecular amide-amide hydrogen bond: variable-temperature NMR and IR studies on a homologous diamide series
Samuel H. Gellman;Gregory P. Dado;Gui Bai Liang;Bruce R. Adams.
Journal of the American Chemical Society (1991)
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