Literature DB >> 15504412

The folding of spectrin domains II: phi-value analysis of R16.

Kathryn A Scott1, Lucy G Randles, Jane Clarke.   

Abstract

Studies on the folding of helical proteins have shown a wide range of different mechanisms and highlighted the importance of helical propensity as a factor in determining folding mechanism. Here, we contribute to this interesting field with the protein engineering phi-value analysis of the 16th domain of chicken brain alpha-spectrin, R16. The fortuitous curvature seen in the unfolding arm of the chevron plot allows us to investigate both early and late events in folding. R16 is the first two-state helical protein for which this has been possible.

Entities:  

Mesh:

Substances:

Year:  2004        PMID: 15504412     DOI: 10.1016/j.jmb.2004.09.023

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  32 in total

1.  Protein folding is mechanistically robust.

Authors:  Jeffrey K Weber; Vijay S Pande
Journal:  Biophys J       Date:  2012-02-21       Impact factor: 4.033

2.  Separating the effects of internal friction and transition state energy to explain the slow, frustrated folding of spectrin domains.

Authors:  Beth G Wensley; Lee Gyan Kwa; Sarah L Shammas; Joseph M Rogers; Stuart Browning; Ziqi Yang; Jane Clarke
Journal:  Proc Natl Acad Sci U S A       Date:  2012-06-18       Impact factor: 11.205

3.  The N-terminal to C-terminal motif in protein folding and function.

Authors:  Mallela M G Krishna; S Walter Englander
Journal:  Proc Natl Acad Sci U S A       Date:  2005-01-18       Impact factor: 11.205

4.  Spectrin R16: broad energy barrier or sequential transition states?

Authors:  Kathryn A Scott; Jane Clarke
Journal:  Protein Sci       Date:  2005-06       Impact factor: 6.725

5.  Examining the influence of linkers and tertiary structure in the forced unfolding of multiple-repeat spectrin molecules.

Authors:  Sterling Paramore; Gregory A Voth
Journal:  Biophys J       Date:  2006-08-04       Impact factor: 4.033

6.  A PDZ domain recapitulates a unifying mechanism for protein folding.

Authors:  Stefano Gianni; Christian D Geierhaas; Nicoletta Calosci; Per Jemth; Geerten W Vuister; Carlo Travaglini-Allocatelli; Michele Vendruscolo; Maurizio Brunori
Journal:  Proc Natl Acad Sci U S A       Date:  2006-12-19       Impact factor: 11.205

7.  Spectrin domains lose cooperativity in forced unfolding.

Authors:  Lucy G Randles; Ross W S Rounsevell; Jane Clarke
Journal:  Biophys J       Date:  2006-11-03       Impact factor: 4.033

8.  Exploring subdomain cooperativity in T4 lysozyme II: uncovering the C-terminal subdomain as a hidden intermediate in the kinetic folding pathway.

Authors:  Jason Cellitti; Rachel Bernstein; Susan Marqusee
Journal:  Protein Sci       Date:  2007-03-30       Impact factor: 6.725

9.  Distinguishing specific and nonspecific interdomain interactions in multidomain proteins.

Authors:  Lucy G Randles; Sarah Batey; Annette Steward; Jane Clarke
Journal:  Biophys J       Date:  2007-09-21       Impact factor: 4.033

10.  How well does a funneled energy landscape capture the folding mechanism of spectrin domains?

Authors:  Robert B Best
Journal:  J Phys Chem B       Date:  2013-08-16       Impact factor: 2.991

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.