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
Fluorescence resonance energy transfer mapping of the fourth of six nucleotide-binding sites of chloroplast coupling factor 1.
TL;DR: Two arrangements of the energy transfer map of coupling factor 1 were found which are compatible with the available data and make different predictions about which sites interact in cooperative catalysis.
47
Circular dichroism evidence for the presence of burst-phase intermediates on the conformational folding pathway of ribonuclease A.
TL;DR: Refolding of the very-fast-folding unfolded species (Uvf) of disulfide-intact bovine pancreatic ribonuclease A has been monitored by circular dichroism and values obtained indicate that IU has no significant secondary structure and presumably differs from Uvf by a local structural rearrangement, while I phi has a substantial population of secondary and tertiary structures.
47
Physics-based potentials for the coupling between backbone- and side-chain-local conformational states in the UNited RESidue (UNRES) force field for protein simulations.
TL;DR: The physics-based counterparts of these potentials are introduced, which are derived from the all-atom energy surfaces of terminally blocked amino-acid residues by Boltzmann integration over the angles λ(1) andλ(2) for rotation about the Cα···Cα virtual-bond angles and over the side-chain angles χ.
47
Conformational unfolding in the N-terminal region of ribonuclease A detected by nonradiative energy transfer: distribution of interresidue distances in the native, denatured, and reduced-denatured states.
TL;DR: Reduced‐denatured ribonuclease A has residual structure that limits segmental Brownian motion in the N‐terminal segment, indicating that large‐scale segmental motions do not take place in the denatured protein within the excited‐state lifetime of the donor.
47
Energy‐based reconstruction of a protein backbone from its α‐carbon trace by a Monte‐Carlo method
TL;DR: An automatic procedure is proposed for reconstruction of a protein backbone from its Cα‐trace; it is based on optimization of a simplified energy function of a peptide backbone, given its α‐carbon trace, and the energy of the structure is minimized with the ECEPP/3 force field.
47