Harold A. Scheraga
Cornell University
1160 Papers
25.6K Citations
Harold A. Scheraga is an academic researcher from Cornell University. The author has contributed to research in topics: Protein structure & Protein folding. The author has an hindex of 120, co-authored 1152 publications. Previous affiliations of Harold A. Scheraga include University of Gdańsk & National University of San Luis.
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Papers
Structure of Water and Hydrophobic Bonding in Proteins. IV. The Thermodynamic Properties of Liquid Deuterium Oxide
TL;DR: In this article, a model for the theoretical derivation of the thermodynamic parameters of liquid water was shown to be applicable to liquid deuterium oxide (D2O), and the calculated structural parameters indicate that more structural order exists in D2O than in H2O at a given temperature.
Role of interchain interactions in the stabilization of the right-handed twist of β-sheets*
TL;DR: Conformational energy computations have been carried out for parallel and antiparallel beta-sheets composed of poly-L-Val and poly- L-Ile peptide chains, each consisting of four and of six residues, respectively, with CH3CO- and-NHCH3 end groups, found to have a large right-handed twist of a magnitude that corresponds to the mean twist of beta-sheet observed in globular proteins.
On the biologically active structures of cholecystokinin, little gastrin, and enkephalin in the gastrointestinal system.
Matthew R. Pincus,Robert P. Carty,James J. Chen,Jack Lubowsky,Matthew Avitable,Dipak Shah,Harold A. Scheraga,Randall B. Murphy +7 more
TL;DR: The biologically active conformations of a series of four peptides and enkephalin in their interactions with gastrointestinal receptors have been deduced using conformational computational analysis and it is found that preferred conformations for the peripherally active peptides CCK-7 and CER-7 are principally beta-bends, whereas little gastrin andCCK-4 are fundamentally helical.
Molecular mechanisms for cooperative folding of proteins
Ming-Hong Hao,Harold A. Scheraga +1 more
TL;DR: A comparative study of the conventional cubic-lattice chain model and a fine-grained more realistic lattice protein model is carried out and two limiting molecular mechanisms for protein folding emerge, which can be used for analyzing the folding process of real proteins.