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
Conformational unfolding in the N-terminal region of ribonuclease A detected by nonradiative energy transfer.
TL;DR: Unfolding in the N-terminal region of RNase A was studied by the nonradiative energy-transfer technique and the efficiencies of energy transfer determined with both fluorescence intensity and lifetime measurements were in reasonably good agreement.
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Improvement of the Treatment of Loop Structures in the UNRES Force Field by Inclusion of Coupling between Backbone- and Side-Chain-Local Conformational States
Paweł Krupa,Adam K. Sieradzan,S. Rackovsky,Maciej Baranowski,Stanisław Ołldziej,Harold A. Scheraga,Adam Liwo,Cezary Czaplewski +7 more
TL;DR: New side-chain-backbone correlation potentials, derived from a statistical analysis of loop regions of 4585 proteins, are introduced to improve the representation of local structure in the coarse-grained UN RESidue model.
Optimization of the UNRES Force Field by Hierarchical Design of the Potential-Energy Landscape. 1. Tests of the Approach Using Simple Lattice Protein Models
Adam Liwo,Piotr Arlukowicz,Stanisław Ołdziej,Cezary Czaplewski,Mariusz Makowski,Harold A. Scheraga +5 more
TL;DR: This paper implemented cubic-lattice models of 12-bead polypeptide chains to study the properties of the recently proposed method for optimizing potential-energy functions for protein-structure prediction and folding simulations and assess its advantage over a single energy gap and Z-score optimization.
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Lysosomal enzyme tripeptidyl peptidase 1 destabilizes fibrillar Aβ by multiple endoproteolytic cleavages within the β-sheet domain.
Santiago Solé-Domènech,Ana Rojas,Gia G. Maisuradze,Harold A. Scheraga,Peter Lobel,Frederick R. Maxfield +5 more
TL;DR: It is demonstrated that tripeptidyl peptidase 1 (TPP1), a lysosomal serine protease, is able to proteolyze fibrillar Aβ efficiently, which is a novel role for TPP1 in the degradation of fibril Aβ that might lead to new approaches to enhance Aβ degradation.
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Elucidating Important Sites and the Mechanism for Amyloid Fibril Formation by Coarse-Grained Molecular Dynamics.
TL;DR: It was found that the correct binding, with native hydrogen bonds, of the free monomer to the fibril template at both stages is crucial for fibrils elongation.
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