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Coexistence of Flexibility and Stability of Proteins: An Equation of State

We consider a recently suggested “equation of state” for natively folded proteins, and verify its validity for a set of about 5800 proteins. The equation is based on a fractal viewpoint of proteins, on a generalization of the Landau-Peierls instability, and on a marginal stability criterion. The lat...

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Detalles Bibliográficos
Autores principales: de Leeuw, Marina, Reuveni, Shlomi, Klafter, Joseph, Granek, Rony
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2754529/
https://www.ncbi.nlm.nih.gov/pubmed/19816577
http://dx.doi.org/10.1371/journal.pone.0007296
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author de Leeuw, Marina
Reuveni, Shlomi
Klafter, Joseph
Granek, Rony
author_facet de Leeuw, Marina
Reuveni, Shlomi
Klafter, Joseph
Granek, Rony
author_sort de Leeuw, Marina
collection PubMed
description We consider a recently suggested “equation of state” for natively folded proteins, and verify its validity for a set of about 5800 proteins. The equation is based on a fractal viewpoint of proteins, on a generalization of the Landau-Peierls instability, and on a marginal stability criterion. The latter allows for coexistence of stability and flexibility of proteins, which is required for their proper function. The equation of state relates the protein fractal dimension [Image: see text], its spectral dimension [Image: see text], and the number of amino acids N. Using structural data from the protein data bank (PDB) and the Gaussian network model (GNM), we compute [Image: see text]and [Image: see text] for the entire set and demonstrate that the equation of state is well obeyed. Addressing the fractal properties and making use of the equation of state may help to engineer biologically inspired catalysts.
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spelling pubmed-27545292009-10-09 Coexistence of Flexibility and Stability of Proteins: An Equation of State de Leeuw, Marina Reuveni, Shlomi Klafter, Joseph Granek, Rony PLoS One Research Article We consider a recently suggested “equation of state” for natively folded proteins, and verify its validity for a set of about 5800 proteins. The equation is based on a fractal viewpoint of proteins, on a generalization of the Landau-Peierls instability, and on a marginal stability criterion. The latter allows for coexistence of stability and flexibility of proteins, which is required for their proper function. The equation of state relates the protein fractal dimension [Image: see text], its spectral dimension [Image: see text], and the number of amino acids N. Using structural data from the protein data bank (PDB) and the Gaussian network model (GNM), we compute [Image: see text]and [Image: see text] for the entire set and demonstrate that the equation of state is well obeyed. Addressing the fractal properties and making use of the equation of state may help to engineer biologically inspired catalysts. Public Library of Science 2009-10-09 /pmc/articles/PMC2754529/ /pubmed/19816577 http://dx.doi.org/10.1371/journal.pone.0007296 Text en de Leeuw et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
de Leeuw, Marina
Reuveni, Shlomi
Klafter, Joseph
Granek, Rony
Coexistence of Flexibility and Stability of Proteins: An Equation of State
title Coexistence of Flexibility and Stability of Proteins: An Equation of State
title_full Coexistence of Flexibility and Stability of Proteins: An Equation of State
title_fullStr Coexistence of Flexibility and Stability of Proteins: An Equation of State
title_full_unstemmed Coexistence of Flexibility and Stability of Proteins: An Equation of State
title_short Coexistence of Flexibility and Stability of Proteins: An Equation of State
title_sort coexistence of flexibility and stability of proteins: an equation of state
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2754529/
https://www.ncbi.nlm.nih.gov/pubmed/19816577
http://dx.doi.org/10.1371/journal.pone.0007296
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