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
Mechanism of action of thrombin on fibrinogen. Direct evidence for the involvement of phenylalanine at position P9.
TL;DR: The presence of Leu (P8) alone is insufficient to account for the enhanced hydrolysis rates and that the presence of Phe (P9) is essential for normal action of thrombin on the A alpha chain of fibrinogen.
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Helix-coil stability constants for the naturally occurring amino acids in water. XXIII. Proline parameters from random poly(hydroxybutylglutamine-CO-L-proline): HELIX-COIL STABILITY CONSTANT. XXIII
TL;DR: The results indicate that L‐proline acts as a very strong helix breaker over the entire temperature range from 0 to 60°C.
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Regeneration of Three-Disulfide Mutants of Bovine Pancreatic Ribonuclease A Missing the 65−72 Disulfide Bond: Characterization of a Minor Folding Pathway of Ribonuclease A and Kinetic Roles of Cys65 and Cys72†
TL;DR: The formation of the 65-72 disulfide loop in the regeneration of wild-type RNase A appears to facilitate the subsequent folding events, and Loop entropy calculations indicate that the increase in the average length of all possibledisulfide loops of the mutants due to the replacement of Cys65 and Cys72 is not sufficient to account for the observed reduction of the values of for the mutants.
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Mechanism of action of thrombin on fibrinogen: The reaction of thrombin with fibrinogen-like peptides containing 11, 14, and 16 residues
TL;DR: The results indicate that phenylanine and leucine at positions P9 and P8 play a key role in the reaction of thrombin with fibrinogen and the data show that factors outside of the 16 residues of peptide C are important in determining the rate of hydrolysis of fibrogen by throm bin.
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