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
Effect of side‐chain hydrophobic bonding on the stability of homopolyamino acid α‐helices: Conformational studies of poly‐L‐leucine in water
TL;DR: From the data for poly‐L‐alanine and theoretical values of the thermodynamic parameters for hydrophobic bond formation, the parameters for formation of a polyglycine helix are computed and separated the contributions of the backbone are obtained.
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Structural characterization of a three-disulfide intermediate of ribonuclease a involved in both the folding and unfolding pathways
TL;DR: The results indicate that des-[65-72]-RNase A has a close structural similarity to RNase A in all regions with the only major differences occurring in a loop region comprising residues 60-72, and suggest that, in the regeneration pathways involving des-[ 65-72], the loop region from 60 to 72 is the last to fold.
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Energy of stabilization of the right-handed βαβ crossover in proteins
TL;DR: In this paper, the authors provided an explanation for the observed nearly exclusive preference of the βαβ structure for forming a right-handed, rather than a left-handed crossover connection.
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Prediction of the native conformation of a polypeptide by a statistical‐mechanical procedure. III. Probable and average conformations of enkephalin
TL;DR: The results of the Monte Carlo calculation of the structure of Met‐enkephalin indicate that the thermodynamically preferred conformation of the pentapeptide contains a γ‐turn involving the three residues Gly2‐Gly3‐Phe4, which further support the conclusion that the γturn conformation is thermodynamic favored.
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