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
Assessing the fractions of tautomeric forms of the imidazole ring of histidine in proteins as a function of pH.
TL;DR: The results for proteins indicate that the protonated form of histidine is the most populated one, whereas the distribution of the tautomeric forms for the imidazole ring varies significantly among different histidines in the same protein, reflecting the importance of the environment of the histidine in determining the tauts.
Localization of segments essential for polymerization and for calcium binding in the gamma-chain of human fibrinogen.
András Váradi,Harold A. Scheraga +1 more
TL;DR: It is concluded that the gamma-chain segment 356/357-411, present in fragment D1 but absent from fragment D2, is essential for maintenance of a polymerization site located in the outer (D) nodule of fibrinogen.
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Mechanism of reductive protein unfolding.
TL;DR: The reductive unfolding of ribonuclease A with dithiothreitol proceeds through parallel pathways with the formation of two well-populated partially-unfolded three-disulphide intermediates, contrary to the current view that protein unfolding generally follows an all-or-none mechanism.
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High-resolution NMR studies of fibrinogen-like peptides in solution: structure of a thrombin-bound peptide corresponding to residues 7-16 of the A.alpha. chain of human fibrinogen
TL;DR: The results provide an explanation for the observations that Asp(7), Phe(8), and Gly(12) are strongly conserved in mammalian fibrinogens and that the mutations of Asp (7) to Asn(7) and of Gly (12) to Val(12), result in delayed release of fibr inopeptide A, producing human bleeding disorders.
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