H
Harold A. Scheraga
Researcher at Cornell University
Publications - 1155
Citations - 68161
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 receiving 66461 citations. Previous affiliations of Harold A. Scheraga include University of Gdańsk & National University of San Luis.
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Journal ArticleDOI
Energy parameters in polypeptides. VII. Geometric parameters, partial atomic charges, nonbonded interactions, hydrogen bond interactions, and intrinsic torsional potentials for the naturally occurring amino acids
Journal ArticleDOI
Monte Carlo-minimization approach to the multiple-minima problem in protein folding.
Zhenqin Li,Harold A. Scheraga +1 more
TL;DR: The Monte Carlo-minimization method has located the lowest-energy minimum thus far reported for the brain pentapeptide [Met5]enkephalin in the absence of water, presumably it is the global minimum-energy structure.
Journal ArticleDOI
Structure of Water and Hydrophobic Bonding in Proteins. I. A Model for the Thermodynamic Properties of Liquid Water
TL;DR: In this paper, the authors derived the thermodynamic parameters of liquid water by means of a statistical thermodynamic treatment, based on the ''flickering cluster'' model proposed by Frank and Wen.
Journal ArticleDOI
Global optimization of clusters, crystals, and biomolecules
TL;DR: Some recent progress in finding the global minima of potential energy functions is described, focusing on applications of the simple "basin-hopping" approach to atomic and molecular clusters and more complicated hypersurface deformation techniques for crystals and biomolecules.
Book ChapterDOI
Experimental and theoretical aspects of protein folding.
Anfinsen Cb,Harold A. Scheraga +1 more
TL;DR: The development of conformational energy calculation procedures will enable the three-dimensional structure of a native protein to be predicted from the knowledge of its amino acid sequence and its interactions with the solvent in which it is dissolved.