Literature DB >> 7568221

Simple model of protein folding kinetics.

R Zwanzig1.   

Abstract

A simple model of the kinetics of protein folding is presented. The reaction coordinate is the "correctness" of a configuration compared with the native state. The model has a gap in the energy spectrum, a large configurational entropy, a free energy barrier between folded and partially folded states, and a good thermodynamic folding transition. Folding kinetics is described by a master equation. The folding time is estimated by means of a local thermodynamic equilibrium assumption and then is calculated both numerically and analytically by solving the master equation. The folding time has a maximum near the folding transition temperature and can have a minimum at a lower temperature.

Mesh:

Year:  1995        PMID: 7568221      PMCID: PMC40890          DOI: 10.1073/pnas.92.21.9801

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  10 in total

1.  The nature of folded states of globular proteins.

Authors:  J D Honeycutt; D Thirumalai
Journal:  Biopolymers       Date:  1992-06       Impact factor: 2.505

2.  Levinthal's paradox.

Authors:  R Zwanzig; A Szabo; B Bagchi
Journal:  Proc Natl Acad Sci U S A       Date:  1992-01-01       Impact factor: 11.205

3.  Implications of thermodynamics of protein folding for evolution of primary sequences.

Authors:  E I Shakhnovich; A M Gutin
Journal:  Nature       Date:  1990-08-23       Impact factor: 49.962

4.  Metastability of the folded states of globular proteins.

Authors:  J D Honeycutt; D Thirumalai
Journal:  Proc Natl Acad Sci U S A       Date:  1990-05       Impact factor: 11.205

Review 5.  Principles of protein folding--a perspective from simple exact models.

Authors:  K A Dill; S Bromberg; K Yue; K M Fiebig; D P Yee; P D Thomas; H S Chan
Journal:  Protein Sci       Date:  1995-04       Impact factor: 6.725

6.  Funnels, pathways, and the energy landscape of protein folding: a synthesis.

Authors:  J D Bryngelson; J N Onuchic; N D Socci; P G Wolynes
Journal:  Proteins       Date:  1995-03

7.  How does a protein fold?

Authors:  A Sali; E Shakhnovich; M Karplus
Journal:  Nature       Date:  1994-05-19       Impact factor: 49.962

Review 8.  Navigating the folding routes.

Authors:  P G Wolynes; J N Onuchic; D Thirumalai
Journal:  Science       Date:  1995-03-17       Impact factor: 47.728

9.  Kinetics of protein folding. A lattice model study of the requirements for folding to the native state.

Authors:  A Sali; E Shakhnovich; M Karplus
Journal:  J Mol Biol       Date:  1994-02-04       Impact factor: 5.469

10.  Spin glasses and the statistical mechanics of protein folding.

Authors:  J D Bryngelson; P G Wolynes
Journal:  Proc Natl Acad Sci U S A       Date:  1987-11       Impact factor: 11.205

  10 in total
  44 in total

1.  A simple model for calculating the kinetics of protein folding from three-dimensional structures.

Authors:  V Muñoz; W A Eaton
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

2.  Hierarchies and logarithmic oscillations in the temporal relaxation patterns of proteins and other complex systems.

Authors:  R Metzler; J Klafter; J Jortner
Journal:  Proc Natl Acad Sci U S A       Date:  1999-09-28       Impact factor: 11.205

3.  Entropic barriers, transition states, funnels, and exponential protein folding kinetics: a simple model.

Authors:  D J Bicout; A Szabo
Journal:  Protein Sci       Date:  2000-03       Impact factor: 6.725

4.  Topology to geometry in protein folding: beta-lactoglobulin.

Authors:  A Fernández; A Colubri; R S Berry
Journal:  Proc Natl Acad Sci U S A       Date:  2000-12-19       Impact factor: 11.205

5.  Heat capacity of protein folding.

Authors:  A Bakk; J S Høye; A Hansen
Journal:  Biophys J       Date:  2001-08       Impact factor: 4.033

Review 6.  From discrete protein kinetics to continuous Brownian dynamics: a new perspective.

Authors:  Hong Qian
Journal:  Protein Sci       Date:  2002-01       Impact factor: 6.725

7.  A semiflexible polymer model applied to loop formation in DNA hairpins.

Authors:  S V Kuznetsov; Y Shen; A S Benight; A Ansari
Journal:  Biophys J       Date:  2001-11       Impact factor: 4.033

8.  Critical nucleation size in the folding of small apparently two-state proteins.

Authors:  Yawen Bai; Hongyi Zhou; Yaoqi Zhou
Journal:  Protein Sci       Date:  2004-04-09       Impact factor: 6.725

9.  Equilibrium unfolding of the PDZ domain of β2-syntrophin.

Authors:  Gabriela María Torchio; Mario Roberto Ermácora; Mauricio Pablo Sica
Journal:  Biophys J       Date:  2012-06-19       Impact factor: 4.033

10.  Role of single-point mutations and deletions on transition temperatures in ideal proteinogenic heteropolymer chains in the gas phase.

Authors:  L Olivares-Quiroz
Journal:  Eur Biophys J       Date:  2016-01-27       Impact factor: 1.733

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