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
UNRES: a united-residue force field for energy-based prediction of protein structure—orgin and significance of multibody terms
Adam Liwo,Jaroslaw Pillardy,Cezary Czaplewski,Jooyoung Lee,Daniel R. Ripoll,Małgorzata Groth,Sylwia Rodziewicz-Motowidło,Rajmund Kamierkiewicz,Ryszard J. Wawak,Stanisław Ołdziej,Harold A. Scheraga +10 more
- 08 Apr 2000
TL;DR: A united-residue force field is developed, hereafter referred to as UNRES, in which a polypeptide chain is represented by a sequence of atoms linked by virtual bonds with attached united side chains and united peptide groups located in the middle between the consecutive β-carbons.
Challenges in structure prediction of oligomeric proteins at the united-residue level: searching the multiple-chain energy landscape with CSA and CFMC.
TL;DR: A revised version of the Conformational Space Annealing (CSA) global optimization method is developed, with three separate measures of structural similarity, in order to overcome the inability of a single distance measure to evaluate multiple‐chain protein structures adequately.
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Minimization of polypeptide energy XII. The methods of partial energies and cubic subdivision
G.M Crippen,Harold A. Scheraga +1 more
TL;DR: In this article, two techniques for finding relatively low minima of the energy of a polypeptide are described: partial energies and cubic subdivision, where high energy regions are eliminated from the space to be searched.
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Ab initio folding of multiple-chain proteins.
Jeffrey A. Saunders,Kenneth D. Gibson,Harold A. Scheraga +2 more
- 01 Dec 2001
TL;DR: The previous methodology for ab initio prediction of protein structure is extended here to treat multiple-chain proteins and good results have been obtained for both a four- and a three-helix protein from the CASP3 exercise.