Designed coiled coils promote folding of a recombinant bacterial collagen - Wikidata - wikimedia - TriplyDB

Designed coiled coils promote folding of a recombinant bacterial collagen

Designed coiled coils promote folding of a recombinant bacterial collagen

http://www.wikidata.org/entity/Q34978886

about

Bacterial collagen-like proteins that form triple-helical structures Vascular Ehlers-Danlos syndrome mutations in type III collagen differently stall the triple helical folding.Circular permutation directs orthogonal assembly in complex collagen peptide mixtures.Location of disorder in coiled coil proteins is influenced by its biological role and subcellular localization: a GO-based study on human proteome.Coiled-Coil Design: Updated and Upgraded.Bioengineered Collagens.Metal Stabilization of Collagen and de Novo Designed Mimetic Peptides Shape-specific nanostructured protein mimics from de novo designed chimeric peptides.Quantum dot display enhances activity of a phosphotriesterase trimer.

P2860

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P2860

Designed coiled coils promote folding of a recombinant bacterial collagen

http://www.wikidata.org/entity/Q34978886

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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name

Designed coiled coils promote folding of a recombinant bacterial collagen

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Designed coiled coils promote folding of a recombinant bacterial collagen

@en

Designed coiled coils promote folding of a recombinant bacterial collagen

@nl

type

label

Designed coiled coils promote folding of a recombinant bacterial collagen

@ast

Designed coiled coils promote folding of a recombinant bacterial collagen

@en

Designed coiled coils promote folding of a recombinant bacterial collagen

@nl

prefLabel

Designed coiled coils promote folding of a recombinant bacterial collagen

@ast

Designed coiled coils promote folding of a recombinant bacterial collagen

@en

Designed coiled coils promote folding of a recombinant bacterial collagen

@nl

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JBC.M110.217364

P1433

Journal of Biological Chemistry

P1476

Designed coiled coils promote folding of a recombinant bacterial collagen

@en

P2093

Aimee L Boyle

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

Anton V Persikov

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

Ayumi Yoshizumi

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

Barbara Brodsky

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

Derek N Woolfson

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

Gail J Bartlett

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

Jordan M Fletcher

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

Thomas L Vincent

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

Zhuoxin Yu

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

P2860

A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants

The Pfam protein families database.

The zipper-like folding of collagen triple helices and the effects of mutations that disrupt the zipper

A periodic table of coiled-coil protein structures.

Rational design of peptide-based building blocks for nanoscience and synthetic biology.

Folding of peptide models of collagen and misfolding in disease.

Expanding the family of collagen proteins: recombinant bacterial collagens of varying composition form triple-helices of similar stability.

A distinct 14 residue site triggers coiled-coil formation in cortexillin I.

The structure of alpha-helical coiled coils.

The design of coiled-coil structures and assemblies.

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17512-17520

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scholarly article

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10.1074/JBC.M110.217364

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20

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286

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3093825

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