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
Kinetics of folding of guanidine-denatured hen egg white lysozyme and carboxymethyl(Cys6,Cys127)-lysozyme: a stopped-flow absorbance and fluorescence study.
TL;DR: Not only does the presence of the disulfide bond between Cys6 and Cys127 slow down the overall folding process of lysozyme, but it also directs the folding of ly sozyme through a pathway characterized by a non-native tertiary interaction(s).
Simple physics-based analytical formulas for the potentials of mean force for the interaction of amino acid side chains in water. IV. Pairs of different hydrophobic side chains.
Mariusz Makowski,Emil Sobolewski,Cezary Czaplewski,Stanisław Ołdziej,Adam Liwo,Harold A. Scheraga +5 more
TL;DR: The potentials of mean force of 21 heterodimers of the molecules modeling hydrophobic amino acid side chains were determined by umbrella-sampling molecular dynamics simulations in explicit water as functions of distance and orientation to justify future use of the determined potentials in coarse-grained protein-folding simulations.
Conformational energy studies of beta-sheets of model silk fibroin peptides. I. Sheets of poly(Ala-Gly) chains.
TL;DR: The computed energies for the two forms of poly(L‐Ala‐Gly) indicate that the silk‐II‐like form is more stable, by about 1.0 kcal/mol per residue, than the well‐established β‐sheet structure of silk II.
Folding and unfolding kinetics of the proline-to-alanine mutants of bovine pancreatic ribonuclease A.
R.W. Dodge,Harold A. Scheraga +1 more
TL;DR: The results from the double-jump stopped-flow experiments indicate that the Tyr92-Ala93 peptide bond in the P93A mutant of RNase A is also cis in the native state, and this model confirms the existence of several previously postulated chain-folding initiation sites.