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
Kinetic folding pathway of a three-disulfide mutant of bovine pancreatic ribonuclease A missing the [40-95] disulfide bond.
Xiaobing Xu,Harold A. Scheraga +1 more
TL;DR: The fitted results indicate that this mutant refolds through a rate-determining step which involves the oxidation of certain two-disulfide species to form a putative three-disolfide species which proceeds rapidly to the native protein.
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Nuclear Overhauser effects and the conformation of gramicidin S.
TL;DR: Using the correlation time and a published relationship between τ c and maximal nuclear Overhauser effect, the observed changes in intensity have been used to derive internuclear distances, which are compared with those predicted from a calculated low energy structure.
34
Improved conformational space annealing method to treat β-structure with the UNRES force-field and to enhance scalability of parallel implementation
Cezary Czaplewski,Cezary Czaplewski,Adam Liwo,Adam Liwo,Jaroslaw Pillardy,Stanisław Ołdziej,Stanisław Ołdziej,Harold A. Scheraga +7 more
TL;DR: In this paper, a hybrid method combining genetic algorithms, essential aspects of the build-up method and a local gradient-based minimization was proposed for the global optimization of protein structures.
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Molecular modeling of the binding modes of the Iron-sulfur protein to the Jac1 co-chaperone from Saccharomyces cerevisiae by all-atom and coarse-grained approaches
TL;DR: The iron‐sulfur protein 1 (Isu1) and the J‐type co‐chaperone Jac1 from yeast are part of a huge ATP‐dependent system, and both interact with Hsp70 chaperones, and two most probable models were subjected to the coarse‐grained molecular dynamics simulations with the UNRES force field.