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
Computer-aided discrimination between active and inactive mutants of the n-terminal domain of the bacteriophage lambda repressor
David C. Kombo,David C. Kombo,George Némethy,George Némethy,Kenneth D. Gibson,Kenneth D. Gibson,S. Rackovsky,S. Rackovsky,Harold A. Scheraga,Harold A. Scheraga +9 more
TL;DR: It is found that the relative orientation of the fifth helices for active mutants is very similar to the wild-type, and that a unique specific orientation pattern of helix-5 relative to helx-5' is required for dimerization-coupled DNA binding activity.
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Limited Proteolysis and Aggregation in the Fibrinogen-Fibrin Conversion
Harold A. Scheraga
- 01 Jan 1961
TL;DR: The fibrinogen–fibrin conversion provides an excellent example of a set of reactions that illustrate the role of side-chain hydrogen bonding in limited proteolysis and in protein association, as part of the process of blood clotting.
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Identification of a new site of conformational heterogeneity in unfolded ribonuclease A.
Marc Adler,Harold A. Scheraga +1 more
TL;DR: There are two slowly exchanging conformational isomers in unfolded bovine pancreatic ribonuclease A (RNase A) in the vicinity of Lys-41, indicating that there are two distinct environments for the dinitrophenyl group.
A conformational study of the tetrapeptide CH3CO-Ala-Asp-Gly-Lys-NHCH3 corresponding to a β-bend in staphylococcal nuclease
TL;DR: The N-acetyl,N′-methylamide derivative of this tetrapeptide is synthesized and its conformation in solution is studied, using nuclear magnetic resonance (NMR) and circular dichroism (CD) spectroscopy.
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Investigation of a physical basis for conformational similarity in proteins.
L. Glasser,Harold A. Scheraga +1 more
TL;DR: Comparison of the smoothed physical factor profiles between sequences, which have similar backbone structures, shows that there is good agreement among the profiles of helical stretches, but not for other backbone structures that have been examined.
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