Literature DB >> 15102453

The protein folding 'speed limit'.

Jan Kubelka1, James Hofrichter, William A Eaton.   

Abstract

How fast can a protein possibly fold? This question has stimulated experimentalists to seek fast folding proteins and to engineer them to fold even faster. Proteins folding at or near the speed limit are prime candidates for all-atom molecular dynamics simulations. They may also have no free energy barrier, allowing the direct observation of intermediate structures on the pathways from the unfolded to the folded state. Both experimental and theoretical approaches predict a speed limit of approximately N/100micros for a generic N-residue single-domain protein, with alpha proteins folding faster than beta or alphabeta. The predicted limits suggest that most known ultrafast folding proteins can be engineered to fold more than ten times faster.

Mesh:

Year:  2004        PMID: 15102453     DOI: 10.1016/j.sbi.2004.01.013

Source DB:  PubMed          Journal:  Curr Opin Struct Biol        ISSN: 0959-440X            Impact factor:   6.809


  297 in total

1.  Variations in the fast folding rates of the lambda-repressor: a hybrid molecular dynamics study.

Authors:  Taras V Pogorelov; Zaida Luthey-Schulten
Journal:  Biophys J       Date:  2004-07       Impact factor: 4.033

2.  Dominant folding pathways of a WW domain.

Authors:  Silvio A Beccara; Tatjana Škrbić; Roberto Covino; Pietro Faccioli
Journal:  Proc Natl Acad Sci U S A       Date:  2012-01-26       Impact factor: 11.205

3.  Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

Authors:  Andrea Soranno; Brigitte Buchli; Daniel Nettels; Ryan R Cheng; Sonja Müller-Späth; Shawn H Pfeil; Armin Hoffmann; Everett A Lipman; Dmitrii E Makarov; Benjamin Schuler
Journal:  Proc Natl Acad Sci U S A       Date:  2012-04-06       Impact factor: 11.205

4.  Chain length determines the folding rates of RNA.

Authors:  Changbong Hyeon; D Thirumalai
Journal:  Biophys J       Date:  2012-02-07       Impact factor: 4.033

5.  Investigating how peptide length and a pathogenic mutation modify the structural ensemble of amyloid beta monomer.

Authors:  Yu-Shan Lin; Gregory R Bowman; Kyle A Beauchamp; Vijay S Pande
Journal:  Biophys J       Date:  2012-01-18       Impact factor: 4.033

6.  Single-molecule observation of helix staggering, sliding, and coiled coil misfolding.

Authors:  Zhiqun Xi; Ying Gao; George Sirinakis; Honglian Guo; Yongli Zhang
Journal:  Proc Natl Acad Sci U S A       Date:  2012-03-26       Impact factor: 11.205

7.  Folding without charges.

Authors:  Martin Kurnik; Linda Hedberg; Jens Danielsson; Mikael Oliveberg
Journal:  Proc Natl Acad Sci U S A       Date:  2012-03-27       Impact factor: 11.205

8.  Connecting energy landscapes with experimental rates for aminoacyl-tRNA accommodation in the ribosome.

Authors:  Paul C Whitford; José N Onuchic; Karissa Y Sanbonmatsu
Journal:  J Am Chem Soc       Date:  2010-09-29       Impact factor: 15.419

9.  Tackling force-field bias in protein folding simulations: folding of Villin HP35 and Pin WW domains in explicit water.

Authors:  Jeetain Mittal; Robert B Best
Journal:  Biophys J       Date:  2010-08-04       Impact factor: 4.033

10.  Dynamics of an ultrafast folding subdomain in the context of a larger protein fold.

Authors:  Caitlin M Davis; R Brian Dyer
Journal:  J Am Chem Soc       Date:  2013-12-13       Impact factor: 15.419

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