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pro vyhledávání: '"Vilá, Jorge"'
Autor:
Vila, Jorge A.
The interconnected processes of protein folding, mutations, epistasis, and evolution have all been the subject of extensive analysis throughout the years due to their significance for structural and evolutionary biology. The origin (molecular basis)
Externí odkaz:
http://arxiv.org/abs/2404.04041
Autor:
Vila, Jorge A.
Proteins have evolved through mutations, amino acid substitutions, since life appeared on Earth, some 109 years ago. The study of these phenomena has been of particular significance because of their impact on protein stability, function, and structur
Externí odkaz:
http://arxiv.org/abs/2310.15779
Autor:
Vila, Jorge A.
One of the main concerns of Anfinsen was to reveal the connection between the amino acid sequence and their biologically active conformation. This search gave rise to two crucial questions in structural biology, namely, why the proteins fold and how
Externí odkaz:
http://arxiv.org/abs/2210.05004
Autor:
Vila, Jorge A.
The Levinthal paradox exposes many critical questions on the protein folding problem, among which we could point out why proteins can reach their native state in a biologically reasonable time. A proper answer to this question is of foremost importan
Externí odkaz:
http://arxiv.org/abs/2208.03150
Autor:
Vila, Jorge A.
The presence of metamorphism in the protein's native state is not yet fully understood. In an attempt to throw light on this issue here we present an assessment, in terms of the amide hydrogen exchange protection factor, that aims to determine the li
Externí odkaz:
http://arxiv.org/abs/2103.00077
Autor:
Vila, Jorge A.
An accurate estimation of the Protein Space size, in light of the factors that govern it, is a long-standing problem and of paramount importance in evolutionary biology, since it determines the nature of protein evolvability. A simple analysis will e
Externí odkaz:
http://arxiv.org/abs/2008.11602
Autor:
Vila, Jorge A.
It is a common belief that metamorphic proteins challenge the Anfinsen thermodynamic hypothesis (or dogma). Here we argue against this view aims to show that metamorphic proteins not just fulfill the Anfinsen dogma but also exhibit marginal stability
Externí odkaz:
http://arxiv.org/abs/2005.01436
Autor:
Martin, Osvaldo A., Vila, Jorge A.
Here we propose that the upper bound marginal stability of proteins (7.4 kcal/mol) is a universal property that includes macro-molecular complexes and is not affected by molecular changes such as mutations and Post-Translational Modifications. Its ex
Externí odkaz:
http://arxiv.org/abs/1907.07524
Autor:
Vila, Jorge A.
Publikováno v:
Physica A 533 (2019) 122053
Use of a combination of statistical thermodynamics and the Gershgorin theorem enable us to guess, in the thermodynamic limit, a plausible value for the upper bound free-energy difference between native-like structures of monomeric globular proteins.
Externí odkaz:
http://arxiv.org/abs/1811.08885
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