Contact order revisited: Influence of protein size on the folding rate

Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chai...

ver descrição completa

Na minha lista:
Detalhes bibliográficos
Main Authors: Ivankov, Dmitry N., Garbuzynskiy, Sergiy O., Alm, Eric, Plaxco, Kevin W., Baker, David, Finkelstein, Alexei V.
Formato: Artigo
Idioma:English
Publicado em: Cold Spring Harbor Laboratory Press 2003
Assuntos:
Article
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC2324001/
https://ncbi.nlm.nih.gov/pubmed/12931003
Tags: Adicionar Tag
Sem tags, seja o primeiro a adicionar uma tag!
id pubmed-2324001
record_format dspace
spelling pubmed-23240012008-05-05 Contact order revisited: Influence of protein size on the folding rate Ivankov, Dmitry N. Garbuzynskiy, Sergiy O. Alm, Eric Plaxco, Kevin W. Baker, David Finkelstein, Alexei V. Protein Sci Article Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L(2/3), and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO × L, is able to predict rather accurately folding rates for both two-state and multistate folding proteins, as well as short peptides, and that this Abs_CO scales with the protein chain length as L(0.70 ± 0.07) for the totality of studied single-domain proteins and peptides. Cold Spring Harbor Laboratory Press 2003-09 /pmc/articles/PMC2324001/ /pubmed/12931003 Text en Copyright © Copyright 2003 The Protein Society
institution US National Library of Medicine
collection PubMed Central
language English
format Article
topic Article
spellingShingle Article
Ivankov, Dmitry N.
Garbuzynskiy, Sergiy O.
Alm, Eric
Plaxco, Kevin W.
Baker, David
Finkelstein, Alexei V.
Contact order revisited: Influence of protein size on the folding rate
description Guided by the recent success of empirical model predicting the folding rates of small two-state folding proteins from the relative contact order (CO) of their native structures, by a theoretical model of protein folding that predicts that logarithm of the folding rate decreases with the protein chain length L as L(2/3), and by the finding that the folding rates of multistate folding proteins strongly correlate with their sizes and have very bad correlation with CO, we reexamined the dependence of folding rate on CO and L in attempt to find a structural parameter that determines folding rates for the totality of proteins. We show that the Abs_CO = CO × L, is able to predict rather accurately folding rates for both two-state and multistate folding proteins, as well as short peptides, and that this Abs_CO scales with the protein chain length as L(0.70 ± 0.07) for the totality of studied single-domain proteins and peptides.
author Ivankov, Dmitry N.
Garbuzynskiy, Sergiy O.
Alm, Eric
Plaxco, Kevin W.
Baker, David
Finkelstein, Alexei V.
author_facet Ivankov, Dmitry N.
Garbuzynskiy, Sergiy O.
Alm, Eric
Plaxco, Kevin W.
Baker, David
Finkelstein, Alexei V.
author_sort Ivankov, Dmitry N.
title Contact order revisited: Influence of protein size on the folding rate
title_short Contact order revisited: Influence of protein size on the folding rate
title_full Contact order revisited: Influence of protein size on the folding rate
title_fullStr Contact order revisited: Influence of protein size on the folding rate
title_full_unstemmed Contact order revisited: Influence of protein size on the folding rate
title_sort contact order revisited: influence of protein size on the folding rate
publisher Cold Spring Harbor Laboratory Press
publisher_facet Cold Spring Harbor Laboratory Press
publishDate 2003
url https://ncbi.nlm.nih.gov/pmc/articles/PMC2324001/
https://ncbi.nlm.nih.gov/pubmed/12931003
_version_ 1760575656241922048

Registos relacionados