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
Resolution enhancement in spectroscopy by maximum entropy fourier self-deconvolution, with applications to Raman spectra of peptides and proteins
Feng Ni,Harold A. Scheraga +1 more
TL;DR: In this paper, a comparative study was made between the maximum entropy (MEM) and the conventional discrete Fourier transform (DFT) methods, and it was pointed out that a combined use of different techniques should be made whenever possible in carrying out digital signal enhancement in order to reduce the chance of misinterpretation of spectral information.
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Geometrical criteria for formation of coiled-coil structures of polypeptide chains.
Ken Nishikawa,Harold A. Scheraga +1 more
TL;DR: It is shown that strong geometrical restrictions exist for the formation of coiled-coil structures from a given minor helix conformation of a polypeptide chain; these restrictions are expressed in a general form that is applicable to any coil of any number of residues in a repeat unit.
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Analysis of $$ {}^{13}{\text{C}}^{{{\upalpha}}} $$ and $$ {}^{13}{\text{C}}^{{{\upbeta}}} $$ chemical shifts of cysteine and cystine residues in proteins: a quantum chemical approach
TL;DR: Martin, Osvaldo Antonio as mentioned in this paper, et al. Consejo Nacional de Investigaciones Cientificas y Tecnicas (CICTE), 2013.
Distance-constraint approach to protein folding. I. Statistical analysis of protein conformations in terms of distances between residues
Hiroshi Wako,Harold A. Scheraga +1 more
TL;DR: In this paper, a statistical analysis of protein conformations in terms of the distance between residues, represented by their Cα atoms, is presented, where the authors consider four factors that contribute to the determination of the distanced====== i,i+k====== between a given pair of residues, and(i +k)th residues in the native conformation of a globular protein.
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