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
Acceleration of oxidative folding of bovine pancreatic ribonuclease A by anion-induced stabilization and formation of structured native-like intermediates
TL;DR: Phosphate anions accelerate the oxidative folding of reduced bovine pancreatic ribonuclease A with dithiothreitol at several temperatures and ionic strengths and the initial equilibration of unstructured disulfide ensembles, presumably due to non‐specific electrostatic and hydrogen bonding effects on the protein and solvent.
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Hairpin bend and interhelical interactions in α-helical poly(l-alanine) in water
TL;DR: Conformational energy calculations were carried out to compute the properties of two antiparallel right-handed α-helical sections (with an intervening hairpin bend) of poly ( l -alanine) in water, and this transition is a favorable one, and may account for the great stability of α- helical poly in water and for the formation of incipient globularity in some proteins.
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Thrombin hydrolysis of an N-terminal peptide from fibrinogen Lille: kinetic and NMR studies.
TL;DR: Electrostatic (or salt-bridge) interactions between Asp(7) and thrombin do not influence the bound conformations of these peptides, and the NMR data indicate no difference in the bound conformation of these two peptides.
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Effects of mutation, truncation, and temperature on the folding kinetics of a WW domain.
TL;DR: Three-state folding is found to be a main mechanism for folding the FBP28 WW domain and most of the full-size and truncated mutants.
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