Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin - Test2 - elhamkhani - TriplyDB

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

http://www.wikidata.org/entity/Q35180560

about

Making muscle elastic: the structural basis of myomesin stretching Superhelical architecture of the myosin filament-linking protein myomesin with unusual elastic properties CARP interacts with titin at a unique helical N2A sequence and at the domain Ig81 to form a structured complex Stable single α-helices are constant force springs in proteins Ultrastable cellulosome-adhesion complex tightens under load.Single molecule force spectroscopy using polyproteins.Towards design principles for determining the mechanical stability of proteins.Titin and obscurin: giants holding hands and discovery of a new Ig domain subset Binding of Myomesin to Obscurin-Like-1 at the Muscle M-Band Provides a Strategy for Isoform-Specific Mechanical Protection.Force-induced remodelling of proteins and their complexes Catch bond-like kinetics of helix cracking: network analysis by molecular dynamics and milestoning.Molecular basis of the mechanical hierarchy in myomesin dimers for sarcomere integrity.Direct Identification of Protein-Protein Interactions by Single-Molecule Force Spectroscopy.Transient-state fluctuationlike relation for the driving force on a biomolecule.Tuning protein mechanics through an ionic cluster graft from an extremophilic protein.Molecular mechanics of coiled coils loaded in the shear geometry.

P2860

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P2860

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

http://www.wikidata.org/entity/Q35180560

description

2011 nî lūn-bûn

@nan

2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

@ast

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

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type

label

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

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Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

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prefLabel

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

@ast

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

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PNAS.1105734108

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Fast-folding alpha-helices as reversible strain absorbers in the muscle protein myomesin

@en

P2093

Felix Berkemeier

http://www.w3.org/2001/XMLSchema#string

Matthias Rief

http://www.w3.org/2001/XMLSchema#string

Morten Bertz

http://www.w3.org/2001/XMLSchema#string

Nikos Pinotsis

http://www.w3.org/2001/XMLSchema#string

Senbo Xiao

http://www.w3.org/2001/XMLSchema#string

P2860

A new 185,000-dalton skeletal muscle protein detected by monoclonal antibodies

Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin

Mechanoenzymatics of titin kinase.

Structural insight into M-band assembly and mechanics from the titin-obscurin-like-1 complex

Myomesin is a molecular spring with adaptable elasticity

The M-band: an elastic web that crosslinks thick filaments in the center of the sarcomere

Purification and biochemical characterization of myomesin, a myosin-binding and titin-binding protein, from bovine skeletal muscle

Dimerisation of myomesin: implications for the structure of the sarcomeric M-band

Molecular structure of the sarcomeric M band: mapping of titin and myosin binding domains in myomesin and the identification of a potential regulatory phosphorylation site in myomesin.

Regulation of skeletal muscle sarcomere integrity and postnatal muscle function by Mef2c

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14139-14144

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scholarly article

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10.1073/PNAS.1105734108

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34

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108

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Matthias Wilmanns

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2011-08-08T00:00:00Z

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51555564

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21825161

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protein folding

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3161521

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