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
New Insights into Protein (Un)Folding Dynamics.
TL;DR: All-atom molecular dynamics simulations of a model protein revealed that strong correlations between the motions of the SCs and the MC occur transiently at 380 K in unfolded segments of the protein and during the simulations of the whole amino-acid sequence at 450 K.
Nonnative isomers of proline-93 and -114 predominate in heat-unfolded ribonuclease A
Marc Adler,Harold A. Scheraga +1 more
TL;DR: Two models for folding RNase A are presented, that are consistent with these new results and the work of previous investigators, are presented here.
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A new approach to empirical intermolecular and conformational potential energy functions. II. Applications to crystal packing, rotational barriers, and conformational analysis.
TL;DR: An empirical potential energy function based on the interactions of electrons and nuclei (EPEN) has been tested on molecules other than those used for its parameterization and indicates that it is reliable for calculating intermolecular interaction energies and low-energy orientations.
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Evolution of physics-based methodology for exploring the conformational energy landscape of proteins.
Harold A. Scheraga,Jaroslaw Pillardy,Adam Liwo,Adam Liwo,Jooyoung Lee,Cezary Czaplewski,Cezary Czaplewski,Daniel R. Ripoll,William J. Wedemeyer,William J. Wedemeyer,Yelena A. Arnautova +10 more
TL;DR: Initial use of a hard‐sphere potential, subsequent more refined force fields, together with efficient methods of global optimization provide indications that progress is being made toward an understanding of the interresidue interactions that underlie protein folding.
Block copolymers of amino acids. I. Synthesis and structure of copolymers of L-alanine or L-phenylalanine with D,L-lysine-d7 or D,L-lysine
TL;DR: Analysis of the amount of the initiator fragment at the C‐terminus of the copolymers was used to obtain the number‐average degrees of polymerization, DPn, and thereby, together with the amino acid composition, to establish the covalent structures of the polymers.
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