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
On the multiple-minima problem in the conformational analysis of polypeptides. II. An electrostatically driven Monte Carlo method--tests on poly(L-alanine).
TL;DR: A new approach to the multiple‐minima problem in protein folding is presented, and its effectiveness by computations on different arbitrary starting conformations of a terminally blocked 19‐residue chain of poly(L‐alanine) for which the global minimum apparently corresponds to the right‐handed α‐helix is illustrated.
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Relation between free energy landscapes of proteins and dynamics.
TL;DR: It is demonstrated how different free energy landscapes (FELs) and folding pathways of trajectories can be, even though they appear to be very similar by visual inspection of the time-dependence of the root-mean-square deviation (rmsd).
Structure of beta-sheets. Origin of the right-handed twist and of the increased stability of antiparallel over parallel sheets.
TL;DR: The minimized energies of parallelβ-sheets are considerably higher than those of the corresponding antiparallel β-sheets, indicating that parallel β-sheet are intrinsically less stable.
156
Physics-based protein-structure prediction using a hierarchical protocol based on the UNRES force field: assessment in two blind tests.
Stanisław Ołdziej,Cezary Czaplewski,Adam Liwo,M. Chinchio,Marian Nanias,Jorge A. Vila,Mey Khalili,Yelena A. Arnautova,A. Jagielska,Mariusz Makowski,H. D. Schafroth,Rajmund Kaźmierkiewicz,Daniel R. Ripoll,Jaroslaw Pillardy,Jeffrey A. Saunders,Young Kee Kang,Kenneth D. Gibson,Harold A. Scheraga +17 more
TL;DR: For target T0198, a phosphate transport system regulator PhoU from T. maritima (a 235-residue mainly alpha-helical protein), the topology of the whole six-helix bundle correctly within 8 A rmsd, except the 32 C-terminal residues, most of which form a beta-hairpin.
156