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
A preliminary three-dimensional structure of angiogenin.
TL;DR: A preliminary three-dimensional structure of angiogenin has been computed, based on its homology to bovine pancreatic ribonuclease A, and a low-energy structure resembling ribonuklease was obtained.
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Lessons from application of the UNRES force field to predictions of structures of CASP10 targets
Yi He,Magdalena A. Mozolewska,Magdalena A. Mozolewska,Paweł Krupa,Paweł Krupa,Adam K. Sieradzan,Tomasz K Wirecki,Tomasz K Wirecki,Adam Liwo,Khatuna Kachlishvili,S. Rackovsky,S. Rackovsky,Dawid Jagieła,Rafał Ślusarz,Cezary Czaplewski,Stanisław Ołdziej,Harold A. Scheraga +16 more
TL;DR: It is shown that the physics-based approach for protein-structure prediction can lead to exceptionally good results when correct domain packing is an issue, even for a highly homologous target, and that it has the ability to predict domain–domain orientations, which is a significant advance in the state of the art.
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Optimization of the UNRES Force Field by Hierarchical Design of the Potential-Energy Landscape. 3. Use of Many Proteins in Optimization
Stanisław Ołdziej,Justyna Ła̧giewka,Adam Liwo,Cezary Czaplewski,M. Chinchio,and Marian Nanias,Harold A. Scheraga +6 more
TL;DR: The application of the hierarchical optimization method of protein potential-energy landscapes described in the accompanying papers to optimize the UNRES potential energy function was successful and the target function composed of con...
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Stereochemical requirements for the existence of hydrogen bonds in β-bends
TL;DR: The possibility of formation of intra-bend hydrogen bonds, involving NH and CO groups, depends on the relative orientation of the peptide groups, and hence differs for various types of bends as mentioned in this paper.
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