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 protein folding
Yuan-Jie Ye,Harold A. Scheraga +1 more
- 10 Apr 2008
TL;DR: In this paper, a Laplace transformation is used to find the global energy minimum on the potential energy hyper-surface of a protein for a two-state model and for three different foldable models as well as for two native proteins.
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Dominance of irregular structures in the formation of intramolecular antiparallel β sheets by homopolyamino acids
TL;DR: A matrix formulation of the conformational partition function is used to assess the influence of irregular structures on the formation of intramolecular antiparallel β sheets, which cause the fibers that are formed to be longer and thicker and have more residues per strand.
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Tracking the Mechanism of Fibril Assembly by Simulated Two-Dimensional Ultraviolet Spectroscopy
TL;DR: To examine the structures in the early time-scale formation and growth of amyloid fibrils, simulated two-dimensional ultraviolet spectroscopy is used and the protein geometry-correlated chiral xxxy signal and the non-chiral combined signal xyxy-xyyx were found to be sensitive to, and in agreement with, a dock/lock pathway.
A generalized G-SFED continuum solvation free energy calculation model
TL;DR: The model proposed in this article, GSFED model, can be used for the solvation free energy calculation of most organic solutes in most organicsolvents and provides an accurate and fast generalized framework without a complicated description of a solution.
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Study of the state of ionization of [leu5]-enkephalin in the crystal and in solution
TL;DR: The state of ionization of [Leu5]-enkephalin in the crystal and in solution was studied with the aid of Raman, i.r., and n.m.r. techniques and the results indicate that, in the Crystal, enkphalin adopts the dipolar ion form.
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