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
Prediction of Conformation of Rat Galanin in the Presence and Absence of Water with the Use of Monte Carlo Methods and the ECEPP/3 Force Field
Adam Liwo,S. Oldziej,Jerzy Ciarkowski,G Kupryszewski,Matthew R. Pincus,Ryszard J. Wawak,S. Rackovsky,Harold A. Scheraga +7 more
TL;DR: The conformation of the 29-residue rat galanin neuropeptide was studied using the Monte Carlo with energy minimization (MCM) and electrostatically driven Monte Carlo (EDMC) methods and results are in qualitative agreement with the available NMR and CD data of galan in aqueous and nonaqueous solvents.
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Conformational studies of the α-helical 28-43 fragment of the B3 domain of the immunoglobulin binding protein G from Streptococcus
Agnieszka Skwierawska,Agnieszka Skwierawska,Sylwia Rodziewicz-Motowidło,Stanisław Ołdziej,Stanisław Ołdziej,Adam Liwo,Adam Liwo,Harold A. Scheraga +7 more
TL;DR: The absence of a stable three-dimensional structure of the investigated peptide supports an earlier study of a possible mechanism for folding of other (B1 and B2) immunoglobulin binding domains of Protein G.
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Search for low-energy conformations of a neurotoxic protein by means of predictive rules, tests for hard-sphere overlaps, and energy minimization*
TL;DR: A method to obtain models for the three-dimensional structure of the neurotoxin alpha from Naja nigricollis from its amino acid sequence is explored, providing an illustration as to how empirical protein algorithms may be used to limit the conformational space, in which energy minimization has to be carried out.
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Solution NMR evidence for a cis Tyr-Ala peptide group in the structure of [Pro93Ala] bovine pancreatic ribonuclease A.
Ying Xiong,Darmawi Juminaga,G.V.T. Swapna,William J. Wedemeyer,Harold A. Scheraga,Gaetano T. Montelione +5 more
TL;DR: Analysis of backbone proton resonance assignments for P93 A together with nuclear Overhauser effect data that provide spectroscopic evidence for a type VI β‐bend conformation with a cis Tyr92‐Ala93 peptide group in the folded structure support the view that a cis Pro93 conformation is crucial for proper folding of wild‐type RNase A.