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Cooperativity between the hydrophobic and cross-linking domains of elastin

Cooperativity between the hydrophobic and cross-linking domains of elastin

http://www.wikidata.org/entity/Q57099498

about

Subtle balance of tropoelastin molecular shape and flexibility regulates dynamics and hierarchical assembly.Conformational transitions of the cross-linking domains of elastin during self-assembly Quantitative comparison of structure and dynamics of elastin following three isolation schemes by 13C solid state NMR and MALDI mass spectrometry.Structural disorder and dynamics of elastin.Shape of tropoelastin, the highly extensible protein that controls human tissue elasticity.Mechanical, structural, and dynamical modifications of cholesterol exposed porcine aortic elastin.Tropoelastin: a versatile, bioactive assembly module.Modular design in natural and biomimetic soft materials.Single nucleotide polymorphisms and domain/splice variants modulate assembly and elastomeric properties of human elastin. Implications for tissue specificity and durability of elastic tissue.

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P2860

Cooperativity between the hydrophobic and cross-linking domains of elastin

http://www.wikidata.org/entity/Q57099498

description

article publié dans la revue scientifique Journal of Biological Chemistry

@fr

im August 2006 veröffentlichter wissenschaftlicher Artikel

@de

scientific article published in Journal of Biological Chemistry

@en

wetenschappelijk artikel

@nl

наукова стаття, опублікована в серпні 2006

@uk

name

Cooperativity between the hydrophobic and cross-linking domains of elastin

@en

Cooperativity between the hydrophobic and cross-linking domains of elastin

@nl

type

label

Cooperativity between the hydrophobic and cross-linking domains of elastin

@en

Cooperativity between the hydrophobic and cross-linking domains of elastin

@nl

prefLabel

Cooperativity between the hydrophobic and cross-linking domains of elastin

@en

Cooperativity between the hydrophobic and cross-linking domains of elastin

@nl

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P1433

Journal of Biological Chemistry

P1476

Cooperativity between the hydrophobic and cross-linking domains of elastin

@en

P2093

Fred W Keeley

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

Joanna P Ho

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

Kristin K Kumashiro

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

Walter P Niemczura

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

P2860

Solid-state nuclear magnetic resonance evidence for an extended beta strand conformation of the membrane-bound HIV-1 fusion peptide.

Solid-state (13)C NMR reveals effects of temperature and hydration on elastin

Nuclear spin-relaxation studies of hydrated elastin.

Quantitative observation of backbone disorder in native elastin.

A relational database for sequence-specific protein NMR data.

Molecular mobility and structure of elastin deduced from the solvent and temperature dependence of 13C magnetic resonance relaxation data.

Elastin: molecular description and function.

Chemical synthesis of cross-linked poly(KGGVG), an elastin-like biopolymer.

Self-aggregation characteristics of recombinantly expressed human elastin polypeptides.

Observation of the glycines in elastin using (13)C and (15)N solid-state NMR spectroscopy and isotopic labeling.

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23757-65

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scholarly article

P356

10.1074/JBC.M510833200

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P407

P433

33

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P478

281

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P577

2006-08-18T00:00:00Z

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16777851

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