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
Crystal Structure Prediction by Global Optimization as a Tool for Evaluating Potentials: Role of the Dipole Moment Correction Term in Successful Predictions
Jaroslaw Pillardy,Ryszard J. Wawak,Yelena A. Arnautova,and Cezary Czaplewski,Harold A. Scheraga +4 more
TL;DR: In this article, a self-consistent basin-to-deformed-basin mapping (S2DBMM) method was proposed to locate a group of large basins containing low-energy minima in the original energy surface.
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Molecular Simulation Study of the Potentials of Mean Force for the Interactions between Models of Like-Charged and between Charged and Nonpolar Amino Acid Side Chains in Water
Katarzyna Maksimiak,Sylwia Rodziewicz-Motowidło,Cezary Czaplewski,Adam Liwo,Harold A. Scheraga +4 more
TL;DR: In this paper, the potentials of mean force (PMF) of the interactions between like-charged and nonpolar amino acid side chains in water were determined to design improved side chain−side chain interaction potentials for our united residue UNRES force field for protein-structure prediction.
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Localization of a fibrin gamma-chain polymerization site within segment Thr-374 to Glu-396 of human fibrinogen.
TL;DR: Fibrinogen fragment D1 was converted to fragment D3 by plasmic digestion and it was found that a 33-residue peptide, corresponding to gamma-chain Thr-374 to Lys-406, binds to immobilized fibrin monomer.
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Kinetic and thermodynamic studies of the folding/unfolding of a tryptophan-containing mutant of ribonuclease A
TL;DR: Refolding data support the hypothesis that the region around position 92 is a chain-folding initiation site in the folding pathway, and the activation energy of the slow-unfolding phase suggested that proline isomerization is involved.
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