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
Prediction of Probable Pathways of Folding in Globular Proteins
TL;DR: The method provides an objective basis for the derivation of a theoretically predicted pathway of protein folding, proposed by us earlier, and can be used both with contact maps derived from a known three-dimensional protein structure and with predicted contact maps computed by means of a statistical procedure from the amino acid sequence alone.
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Conformational analysis of possible biologically active (receptor-bound) conformations of peptides derived from cholecystokinin, cerulein and little gastrin and the opiate peptide, Met-enkephalin.
Matthew R. Pincus,Randall B. Murphy,Robert P. Carty,James M. Chen,Dipak Shah,Harold A. Scheraga +5 more
TL;DR: Possible biologically active (receptor-bound) conformations of peptides derived from cholecystokinin (CCK) have been deduced using conformational analysis combined with comparative studies of their biological specificities.
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A comparison of the predicted and X-ray structures of angiogenin. Implications for further studies of model building of homologous proteins
Simon C. Allen,K. Ravi Acharya,Kathleen A. Palmer,Robert Shapiro,Bert L. Vallee,Harold A. Scheraga +5 more
TL;DR: Comparison of the predicted model and crystal structure shows that the active-site histidine residues and the core of the angiogenin molecule, including most of theβ-strands andα-helices, were predicted reasonably well, however, the structure of the surface loop regions and residues near the truncated C-terminus differs significantly.
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Simultaneous Characterization of the Reductive Unfolding Pathways of RNase B Isoforms by Top-Down Mass Spectrometry
TL;DR: A novel method for characterization of the simultaneous reductive unfolding pathways of five isoforms of bovine pancreatic ribonuclease B (RNase B) is demonstrated, indicating that the unfolding events necessary to expose disulfide bonds for reduction are not affected by the oligosaccharide.
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Effect of protein disulfide isomerase on the regeneration of bovine ribonuclease A with dithiothreitol.
TL;DR: The present results indicate that PDI does not alter the two major parallel pathways involving des‐[65‐72] and des‐,[40‐95] in the regeneration of ribonuclease A with DTT.
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