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
Use of Benzyl Mercaptan for Direct Preparation of Long Polypeptide Benzylthio Esters as Substrates of Subtiligase
Ervin Welker,Harold A. Scheraga +1 more
TL;DR: This approach can successfully extend the current limit of the subtiligase-catalyzed fragment condensation method as well as provide another application of the recently discovered intein chemistry.
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Identifying native-like protein structures with scoring functions based on all-atom ECEPP force fields, implicit solvent models and structure relaxation.
TL;DR: In this article, the results of benchmark tests for scoring functions based on two all-atom ECEPP force fields and two implicit solvent models for a large set of protein decoys are reported.
Conformational properties of 2,4-methanoproline (2-carboxy-2,4-methanopyrrolidine) in peptides: evidence for 2,4-methanopyrrolidine asymmetry based on solid-state x-ray crystallography, proton NMR in aqueous solution, and CNDO/2 conformational energy calculations
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Statistical mechanics of noncovalent bonds in polyamino acids. I. Hydrogen bonding of solutes in water, and the binding of water to polypeptides
TL;DR: In this article, the authors used the Nemethy-Scheraga theory of water structure to calculate the energy changes for the rupture of a solute-solute hydrogen bond in water and a partition function was also obtained for the binding of water and other solutes to the DH and A groups in the special case of a random coil polypeptide chain.
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Proline isomerization in bovine pancreatic ribonuclease A. 1. Unfolding conditions.
TL;DR: It is proposed here that Lys113 in the latter protein interferes with the isomerization of the Lys113-Pro114 peptide group, providing an optical technique by which these well-defined molecular folding events can be studied, under both folding and unfolding conditions, and compared to molecular simulations.
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