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
Exploring the parameter space of the coarse-grained UNRES force field by random search: selecting a transferable medium-resolution force field.
TL;DR: The results demonstrate that, in addition to finding reasonable initial starting points for optimization, an extensive search of parameter space is a powerful method to produce a transferable force field.
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Replica Exchange and Multicanonical Algorithms with the Coarse-Grained United-Residue (UNRES) Force Field
TL;DR: Calculated thermodynamic averages, such as canonical average energy and heat capacity, are in good agreement among all simulations for poly-L-alanine, showing that the algorithms were implemented correctly, and that all three algorithms are equally effective for small systems.
WeFold: a coopetition for protein structure prediction.
George A. Khoury,Adam Liwo,Firas Khatib,Firas Khatib,Hongyi Zhou,Gaurav Chopra,Gaurav Chopra,Jaume Bacardit,Leandro Oliveira Bortot,Rodrigo Antonio Faccioli,Xin Deng,Yi He,Paweł Krupa,Paweł Krupa,Jilong Li,Magdalena A. Mozolewska,Magdalena A. Mozolewska,Adam K. Sieradzan,James Smadbeck,Tomasz K Wirecki,Tomasz K Wirecki,Seth Cooper,Jeff Flatten,Kefan Xu,David Baker,Jianlin Cheng,Alexandre C. B. Delbem,Christodoulos A. Floudas,Chen Keasar,Michael Levitt,Zoran Popović,Harold A. Scheraga,Jeffrey Skolnick,Silvia Crivelli,Foldit Players +34 more
TL;DR: The first attempt at “coopetition” in scientific research applied to the protein structure prediction and refinement problems is presented and both successes and areas needing improvement as identified throughout the first WeFold experiment are described.
Empirical solvation models in the context of conformational energy searches: Application to bovine pancreatic trypsin inhibitor
TL;DR: The behaviour of threeuum solvation models has been examined by applying them to the minimization of the conformational energy of bovine pancreatic trypsin inhibitor.
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Nonrandom Distribution of the One-Disulfide Intermediates in the Regeneration of Ribonuclease A†
TL;DR: The one-disulfide intermediates formed during the oxidative refolding of ribonuclease A (RNase A) have been characterized and all four native disulfide pairings have populations greater than those predicted by loop entropy calculations, suggesting the presence of enthalpic contributions stabilizing these species.
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