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.
Chat about Author
Papers
Statistical mechanics of noncovalent bonds in polyamino acids. IV. Matrix treatment of hydrophobic bonds in the random coil and of the helix–coil transition for chains of arbitrary length†
TL;DR: In this article, the Lifson-Roig matrix theory of the helix-coil transition in polyglycine was extended to situations where side-chain interactions (hydrophobic bonds) are present both in the α-helix and in the random coil, as discussed for short chains in this series.
18
The action of x-rays on fibrinogen solutions.
Harold A. Scheraga,L.F. Nims +1 more
TL;DR: It seems evident, therefore, that the split fragments resulting from the x-irradiation contain the groups necessary for the clotting reaction and that these are probably not those easily oxidized by OH radicals.
18
Immunochemical determination of conformational equilibria for fragments of the B beta chain of fibrinogen.
TL;DR: Kconf, the equilibrium constant for the interconversion of the nonnative and native conformations of this determinant, was determined by measuring the competition between 125I-F and the fibrinogen derivatives under study for binding to the purified antibody.
17
Mechanism of action of thrombin on fibrinogen: NMR evidence for a beta-bend at or near fibrinogen A alpha Gly(P5)-Gly(P4).
TL;DR: Results suggest that there is a beta-bend at Gly(P5)-Gly(P4), possibly stabilized by salt links between Asp(P10) andArg(P3') and between phosphorylated Ser(P14) and Arg(P7'), which brings Phe(P9) close to the hydrolyzable Arg-Gly bonds.
17
Revised Backbone-Virtual-Bond-Angle Potentials to Treat the l- and d-Amino Acid Residues in the Coarse-Grained United Residue (UNRES) Force Field.
TL;DR: The ability of the extended UNRES force field to reproduce thermodynamics of polypeptide systems with d-amino-acid residues was tested by comparing the experimentally measured and the calculated free energies of helix formation of model KLALKLALxxLKLALKLA peptides, where x denotes any d- or l- amino-acid residue.
17