Max Vasquez
Cornell University
10 Papers
279 Citations
Max Vasquez is an academic researcher from Cornell University. The author has contributed to research in topics: Peptide sequence & Helix–coil transition model. The author has an hindex of 9, co-authored 10 publications.
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Papers
High-resolution NMR studies of fibrinogen-like peptides in solution: structure of a thrombin-bound peptide corresponding to residues 7-16 of the A.alpha. chain of human fibrinogen
TL;DR: The results provide an explanation for the observations that Asp(7), Phe(8), and Gly(12) are strongly conserved in mammalian fibrinogens and that the mutations of Asp (7) to Asn(7) and of Gly (12) to Val(12), result in delayed release of fibr inopeptide A, producing human bleeding disorders.
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Helix-coil transition theory including long-range electrostatic interactions: application to globular proteins.
TL;DR: An extension of the Zimm–Bragg two‐state theory for the helix–coil transition in polypeptides, which takes into account the effect of peptide charge–dipole interactions on helix stability, is presented.
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Effect of sequence-specific interactions on the stability of helical conformations in polypeptides.
Max Vasquez,Harold A. Scheraga +1 more
TL;DR: A modification of the Zimm–Bragg two‐state model for the helix–coil transition in polypeptides, which considers the effect of charge–dipole, charge–charge, and other specific interactions on helix stability, is presented.
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Stability of polypeptide conformational states as determined by computer simulation of the free energy.
TL;DR: The method is applied to a model of decaglycine with rigid geometry, using the potential energy function ECEPP (Empirical Conformational Energy Program for Peptides), and the results show that the α‐helix is a more stable structure than the hairpin.
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On the multiple-minima problem in the conformational analysis of polypeptides. V. Application of the self-consistent electrostatic field and the electrostatically driven Monte Carlo methods to bovine pancreatic trypsin inhibitor.
TL;DR: A limited portion of the conformational energy hyperspace of the small protein bovine pancreatic trypsin inhibitor (BPTI) is explored with the aid of two search methods developed in this laboratory, resulting in a series of low‐energy conformations.
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