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
Regeneration of RNase A from the reduced protein: models of regeneration pathways.
TL;DR: The folding of other proteins, accompanying oxidation of the reduced form, and the folding of denatured proteins with intact disulfide bonds are discussed in terms of the growth- and rearrangement-type models.
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Toward an understanding of the folding of ribonuclease A
TL;DR: It is shown here that recent criticisms of results of ribonuclease A regeneration are due to a misinterpretation of the analysis of the data.
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Ultrarapid mixing experiments shed new light on the characteristics of the initial conformational ensemble during the folding of ribonuclease A
Ervin Welker,Kosuke Maki,M. C. Ramachandra Shastry,Darmawi Juminaga,Rajiv Bhat,Harold A. Scheraga,Heinrich Roder +6 more
TL;DR: The isomerization state of proline peptide bonds can have a major impact on the structural events during early stages of folding if RNase A is allowed to equilibrate under denaturing conditions.
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Effect of sequence-specific interactions on the stability of helical conformations in polypeptides.
Max Vasquez,Harold A. Scheraga +1 more
TL;DR: A modification of the Zimm–Bragg two‐state model for the helix–coil transition in polypeptides, which considers the effect of charge–dipole, charge–charge, and other specific interactions on helix stability, is presented.
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Structure-function studies of murine epidermal growth factor: expression and site-directed mutagenesis of epidermal growth factor gene.
Prabir Ray,Franklin J. Moy,Gaetano T. Montelione,Gaetano T. Montelione,Jin Fu Liu,Saran A. Narang,Harold A. Scheraga,Ray Wu +7 more
TL;DR: The data demonstrate the importance of the highly conserved Leu47 residue in mEGF for full biological activity as well as the reduced specific activities in both bioassays.
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