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
Protein structure prediction with the UNRES force-field using replica-exchange monte carlo-with-minimization; comparison with MCM, CSA, and CFMC
Marian Nanias,M. Chinchio,Stanisław Ołdziej,Stanisław Ołdziej,Cezary Czaplewski,Cezary Czaplewski,Harold A. Scheraga +6 more
TL;DR: REMCM was applied to search the conformational space of coarse grain protein systems described by the UNRES force field, and it located global minima for four proteins faster and more consistently than either MCM or CFMC, and the results were compared to those from other optimization methods.
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Hydrogen bonding involving the ornithine side chain of gramicidin S.
TL;DR: The side-chain and backbone hydrogen bonding pattern is identical in the computed minimum-energy conformation of gramicidin S and in the recently determined X-ray crystallographic structure of the hydrated urea complex of this peptide.
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Mechanism of action of thrombin on fibrinogen. Reaction of the N-terminal CNBr fragment from the Aalpha chain of human fibrinogen with bovine thrombin.
TL;DR: The ratio of the Michaelis-Menten constants was found to be 3 × 10−7 [(NIH unit/liter)s]−1, indicating that the Bβ fragment is a poor substrate for thrombin compared to the corresponding Aα chain fragment, and it is suggested that some of the binding sites that are used in the hydrolysis of the B β chain are assumed to be located on either the α or γ chains of fibrinogen.
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Peptide mapping of bovine pancreatic ribonuclease a by reverse-phase high-performance liquid chromatography. I: Application to the reduced and S-carboxymethylated protein
Charles A. McWherter,Theodore W. Thannhauser,Robert A. Fredrickson,Michelle T. Zagotta,Harold A. Scheraga +4 more
TL;DR: Complete peptide maps of reduced and S-carboxymethylated ribonuclease A were obtained by reverse-phase high-performance liquid chromatography with the following peptide-chain cleavage techniques, and S. aureus protease exhibited a broader specificity than had previously been reported.
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Molecular origin of anticooperativity in hydrophobic association.
TL;DR: The packing and orientation of water molecules in the vicinity of the solute and the effect of ordering of the water around nonpolar solutes on many-body interactions are analyzed to explain multibody effects in hydrophobic association on a molecular level.
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