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
Theoretical and Experimental Aspects of Protein Folding
Harold A. Scheraga
- 01 Jan 1983
TL;DR: Scheraga et al. as mentioned in this paper presented the second and third lecture of the International Summer School of Biophysics (ILSB) on protein conformation, where they described some of their theoretical and experimental work designed to gain an understanding of the interactions that lead to the observed conformational behavior of biological macromolecules either as individual molecules or as complexes with other molecules.
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Location of the three buried tyrosyl groups of ribonuclease A.
Chul-Yung Cha,Harold A. Scheraga +1 more
TL;DR: Initial data is reported on the location of the positions of the three iodinated groups in the amino acid sequence of ribonuclease A to form derivative A.
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Combined-information protein structure refinement: Potential energy-constrained real-space method for refinement with limited diffraction data
TL;DR: A potential energy-constrained real-space refinement method designed for use with x-ray diffraction data of low to moderate resolution has been developed and the structure of bovine pancreatic trypsin inhibitor was refined by using this method with data to only 2.5-A resolution.
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Nuclear magnetic resonance study of the side-chain conformation of α-helical poly-β-benzyl-l-aspartate
TL;DR: Denaturation studies indicate that, in contrast to right-handed α-helical poly-γ-benzyl- l -glutamate, the phenyl ring does not play a major part in stabilizing the left-handed β-helix of poly-β-ben ZL -aspartate, which is based on the lack of any noticeable shift in side-chain resonances due to the anisotropic magnetic field of the Phenyl ring.
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Helix‐coil stabilities of L‐alanine and L‐leucine in mixed organic solvents
TL;DR: In this paper, the authors determined the values of the parameters u and s of the Zimm-Bragg theory for several amino acids in aqueous solution, using the "host-guest" technique.
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