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 statistical analysis of side-chain conformations in proteins: Comparison with ECEPP predictions
Akbar Nayeem,Harold A. Scheraga +1 more
TL;DR: ECEPP/3 calculations, carried out after elongating the backbone chain of the model peptide unit, result in distributions that are often closer to the observed side-chain distributions, and the implications for the relative importance of short-range versus long-range interactions in determining protein structure are discussed.
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Impact of an easily reducible disulfide bond on the oxidative folding rate of multi-disulfide-containing proteins.
TL;DR: The studies reveal that the susceptibility of the (40-95) disulfide bond of Y92G bovine pancreatic ribonuclease A (RNase A) to reduction results in a reduced rate of oxidative regeneration, compared with wild-type RNase A.
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Detecting native folds in mixtures of proteins that contain disulfide bonds.
Mahesh Narayan,Ervin Welker,Huili Zhai,Xuemei Han,Guoqiang Xu,Fred W. McLafferty,Harold A. Scheraga +6 more
TL;DR: This work demonstrates a method, which combines mass spectrometry with mild reductions, which requires no prior experimentation or knowledge of proteins' physicochemical characteristics, function or activity, and is amenable to automation for structural genomics and proteomics applications.
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Investigation of Phosphorylation-Induced Folding of an Intrinsically Disordered Protein by Coarse-Grained Molecular Dynamics.
Adam K. Sieradzan,Anatolii Korneev,Alexander Begun,Khatuna Kachlishvili,Harold A. Scheraga,Alexander Molochkov,Patrick Senet,Patrick Senet,Antti J. Niemi,Gia G. Maisuradze +9 more
TL;DR: In this article, the principles that govern the folding of eIF4E-binding protein isoform 2 are investigated by analyzing canonical and replica exchange molecular dynamics trajectories, generated with the coarse-grained united residual force field, in terms of local and global motions and the time dependence of formation of contacts between Cαs of selected pairs of residues.
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