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
A method for optimizing potential-energy functions by a hierarchical design of the potential-energy landscape: application to the UNRES force field.
Adam Liwo,Piotr Arlukowicz,Cezary Czaplewski,Stanisław Ołdziej,Jaroslaw Pillardy,Harold A. Scheraga +5 more
TL;DR: The method was tested on two proteins, PDB ID codes 1FSD and 1IGD, with an off-lattice united-residue force field and found the native structure very quickly, as opposed to the potential-energy functions obtained by former optimization methods.
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Prediction of the native conformation of a polypeptide by a statistical-mechanical procedure. I. Backbone structure of enkephalin.
TL;DR: Initial results on the backbone structure of Met‐enkephalin indicate that an equilibrium statistical‐mechanical procedure, coupled with an adaptive Monte Carlo algorithm, can overcome many of the problems associated with the standard methods of direct energy minimization.
123
A new force field (ECEPP-05) for peptides, proteins, and organic molecules.
TL;DR: The charge model has a stronger effect on the conformational energies than the 1-4 scaling, and the entire force field was demonstrated by reproducing the main energy minima of terminally blocked Ala3 from the literature.
121
Conformational Energy Calculations on Polypeptides and Proteins
TL;DR: In this paper, a summary of five of these methods, namely, build-up, Monte Carlo-plus-minimization (MCM), relaxation of dimensionality, pattern-recognition-based importance sampling minimization (PRISM), and diffusion equation method, are presented.
121
Conformations of cyclo(L‐alanyl‐L‐alanyl‐ε‐aminocaproyl) and of cyclo(L‐alany1‐D‐alanyl‐ε‐aminocaproyl); cyclized dipeptide models for specific types of β‐bends
J. Bandekar,David J. Evans,Samuel Krimm,Sydney J. Leach,S. Lee,J. R. McQuie,Elizabeth Minasian,George Némethy,Marcia S. Pottle,Harold A. Scheraga,E. R. Stimson,R. W. Woody +11 more
TL;DR: In this article, a normal mode analysis of the vibrations of the computed low-energy conformations was compared with solid state infrared and Raman spectra, in order to determine the predominant conformations.
120