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
Conformational characterization of a single-site mutant of murine epidermal growth factor (EGF) by 1H NMR provides evidence that leucine-47 is involved in the interactions with the EGF receptor
TL;DR: The NMR data demonstrate that the significant differences in the binding activities of wild-type and [Ser47]mEGF cannot be attributed to structural changes remote from the three-dimensional site of mutation, and Leu-47 and/or residues spatially adjacent to Lee-47 constitute part of the active site of mEGF.
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Minimization of polypeptide energy. II. Preliminary structures of oxytocin, vasopressin, and an octapeptide from ribonuclease
TL;DR: The expression for the energy of a polypeptide in aqueous solution is extended to take account of the presence of disulfide bridges, and the minimization technique is applied to obtain apparent local energy minima for oxytocin and vasopressin.
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Assessing the accuracy of protein structures by quantum mechanical computations of 13C(alpha) chemical shifts.
Jorge A. Vila,Harold A. Scheraga +1 more
TL;DR: A recently introduced physics-based methodology that makes use of observed and computed (13)C(alpha) chemical shifts for an accurate validation of protein structures in solution and in crystals, and enables local validation by identifying a set of individual amino acid conformations that may represent a nonreliable fold of the protein model.
Distance-constraint approach to protein folding. II. Prediction of three-dimensional structure of bovine pancreatic trypsin inhibitor
Hiroshi Wako,Harold A. Scheraga +1 more
TL;DR: In this paper, the authors examined the possibility of predicting the three-dimensional structure of bovine pancreatic trypsin inhibitor (BPTI) using a distance-constraint approach.
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