Literature DB >> 12618784

The myosin coiled-coil is a truly elastic protein structure.

Ingo Schwaiger1, Clara Sattler, Daniel R Hostetter, Matthias Rief.   

Abstract

Coiled-coils occur in a variety of proteins involved in mechanical and structural tasks in the cell. Their mechanical properties are important in various contexts ranging from hair elasticity to synaptic fusion. Beyond their importance in biology, coiled-coils have also attracted interest as programmable protein sequences for the design of novel hydrogels and materials. We have studied the elastic properties of the myosin coiled-coil at the single molecule level. The coiled-coil undergoes a massive structural transition at forces between 20 and 25 pN where the coil extends to about 2.5 times its original length. Unlike all other proteins investigated mechanically so far, this transition is reversible on a timescale of less than a second, making the coiled-coil a truly elastic protein.

Entities:  

Mesh:

Substances:

Year:  2002        PMID: 12618784     DOI: 10.1038/nmat776

Source DB:  PubMed          Journal:  Nat Mater        ISSN: 1476-1122            Impact factor:   43.841


  74 in total

1.  Mechanism of fibrin(ogen) forced unfolding.

Authors:  Artem Zhmurov; Andre E X Brown; Rustem I Litvinov; Ruxandra I Dima; John W Weisel; Valeri Barsegov
Journal:  Structure       Date:  2011-11-09       Impact factor: 5.006

2.  Pseudoelastic behaviour of a natural material is achieved via reversible changes in protein backbone conformation.

Authors:  Matthew J Harrington; S Scott Wasko; Admir Masic; F Dieter Fischer; Himadri S Gupta; Peter Fratzl
Journal:  J R Soc Interface       Date:  2012-06-13       Impact factor: 4.118

3.  Dynamics of the coiled-coil unfolding transition of myosin rod probed by dissipation force spectrum.

Authors:  Yukinori Taniguchi; Bhavin S Khatri; David J Brockwell; Emanuele Paci; Masaru Kawakami
Journal:  Biophys J       Date:  2010-07-07       Impact factor: 4.033

4.  Stiffening of individual fibrin fibers equitably distributes strain and strengthens networks.

Authors:  Nathan E Hudson; John R Houser; E Timothy O'Brien; Russell M Taylor; Richard Superfine; Susan T Lord; Michael R Falvo
Journal:  Biophys J       Date:  2010-04-21       Impact factor: 4.033

5.  Evidence that αC region is origin of low modulus, high extensibility, and strain stiffening in fibrin fibers.

Authors:  John R Houser; Nathan E Hudson; Lifang Ping; E Timothy O'Brien; Richard Superfine; Susan T Lord; Michael R Falvo
Journal:  Biophys J       Date:  2010-11-03       Impact factor: 4.033

6.  Mechanical response and conformational amplification in α-helical coiled coils.

Authors:  Osman N Yogurtcu; Charles W Wolgemuth; Sean X Sun
Journal:  Biophys J       Date:  2010-12-15       Impact factor: 4.033

7.  Mapping the energy landscape for second-stage folding of a single membrane protein.

Authors:  Duyoung Min; Robert E Jefferson; James U Bowie; Tae-Young Yoon
Journal:  Nat Chem Biol       Date:  2015-10-19       Impact factor: 15.040

8.  Forced unfolding of proteins within cells.

Authors:  Colin P Johnson; Hsin-Yao Tang; Christine Carag; David W Speicher; Dennis E Discher
Journal:  Science       Date:  2007-08-03       Impact factor: 47.728

9.  Exploring the energy landscape of GFP by single-molecule mechanical experiments.

Authors:  Hendrik Dietz; Matthias Rief
Journal:  Proc Natl Acad Sci U S A       Date:  2004-11-05       Impact factor: 11.205

10.  Extensibility of the extended tail domain of processive and nonprocessive myosin V molecules.

Authors:  Attila Nagy; Grzegorz Piszczek; James R Sellers
Journal:  Biophys J       Date:  2009-12-16       Impact factor: 4.033

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.