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 new method for rapid characterization of the folding pathways of multidisulfide-containing proteins.
TL;DR: The results suggest that the stability of the three-dimensional structure of the native protein is a major determinant of the folding rate in oxidative folding.
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Interaction of a biomolecule with mobile ions in aqueous solution: comparison of three fast approximate methods with the direct solution of the nonlinear Poisson-Boltzmann equation
TL;DR: In this paper, three fast approximate methods are introduced to treat the electrostatic effect of the solvent and mobile ions on a biomolecule solute, and they choose the particular method according to the available computer resources and the complexity of the system being modeled.
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Role of interstrand loops in the formation of intramolecular cross‐β‐sheets by homopolymino acids
TL;DR: The matrix treatment of the formation of intramolecular anti‐parallel β‐sheets from a statistical coil has been extended to incorporate interstrand loops of arbitrary size to make it more difficult to complete the final stages of sheet formation.
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Effect of Mutation of Proline 93 on Redox Unfolding/Folding of Bovine Pancreatic Ribonuclease A†
TL;DR: Results demonstrate that the reduction of the P93A mutant proceeds through a local unfolding event and provides strong support for the model in which the Reduction of wild-type RNase A to the des species proceeds through two independent local conformational unfolding events.
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Computational study of packing a collagen-like molecule: Quasi-hexagonal vs “Smith” collagen microfibril model
TL;DR: The lateral packing of a collagen‐like molecule, CH3CO‐(Gly‐L‐Pro‐ L‐Pro)4‐NHCH3, has been examined by energy minimization with the ECEPP/3 force field and is found to be energetically more favorable than the Smith microfibril model.
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