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
Molecular theory of the helix-coil transition in polyamino acids. V. Explanation of the different conformational behavior of valine, isoleucine, and leucine in aqueous solution
Mitiko Gō,Harold A. Scheraga +1 more
TL;DR: The origin of this behavioral difference was examined by computing theoretical values of s versus temperature from interatomic interaction energies, taking solvent (hydrophobic and hydrophilic) effects into account and the calculated s versusTemperature curves for both homopolymers are consistent with the observed experimental behavior.
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Calculation of the Conformation of cyclo-Hexaglycyl. 2. Application of a Monte-Carlo Method
Nobuhiro Gō,Harold A. Scheraga +1 more
TL;DR: In this paper, a Monte-Carlo method is used in a conformational energy analysis of cyclo-hexaglycyl. This method simulates, in an approximate way, the real process in which the molecule changes its conformation in solution.
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Simple Physics-Based Analytical Formulas for the Potentials of Mean Force of the Interaction of Amino Acid Side Chains in Water. VII. Charged–Hydrophobic/Polar and Polar–Hydrophobic/Polar Side Chains
TL;DR: The physics-based potentials of side-chain-side-chain interactions corresponding to pairs composed of charged and polar, polar and Polar, charged and Hydrophobic, and hydrophobic andHydrophobic side chains have been determined.
Kinetic studies of the regeneration of recombinant hirudin variant 1 with oxidized and reduced dithiothreitol
TL;DR: The analysis reveals that the rate-determining step in the regeneration of rHV1 with oxidized and reduced dithiothreitol involves the oxidation of one or more two-disulfide-containing species, most likely those already containing two native disulfide bonds.
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Statistical mechanics of noncovalent bonds in polyamino acids. II. Combinatorial formulation for short chains, including hydrophobic bonding in random coil†
TL;DR: In this article, a combinatorial formulation of the partition function is developed for short polypeptide chains, where summations can be evaluated, and it is shown that it is an excellent approximation to consider the hydrogen-bonded portion of a short (20 residues) chain as consisting of a single helical sequence, with all sizes of helical sequences being about equally probable at the transition temperature.
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