Conservation of folding and association within a family of spidroin N-terminal domains.

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Two-step self-assembly of a spider silk molecular clamp

P2860

Q59131872-8E71E20E-5699-4753-9252-0DF4A9C22670

P2860

Conservation of folding and association within a family of spidroin N-terminal domains.

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Conservation of folding and association within a family of spidroin N-terminal domains.

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Conservation of folding and association within a family of spidroin N-terminal domains.

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Item

label

Conservation of folding and association within a family of spidroin N-terminal domains.

@en

Conservation of folding and association within a family of spidroin N-terminal domains.

@nl

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Conservation of folding and association within a family of spidroin N-terminal domains.

@en

Conservation of folding and association within a family of spidroin N-terminal domains.

@nl

P1476

Conservation of folding and association within a family of spidroin N-terminal domains.

@en

P2093

Charlotte Rat

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

Christopher M Johnson

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

Hannes Neuweiler

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

Julia C Heiby

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

Suhaila Rajab

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

P2860

Self-assembly of spider silk proteins is controlled by a pH-sensitive relay

A conserved spider silk domain acts as a molecular switch that controls fibre assembly

pH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain

Sequential pH-driven dimerization and stabilization of the N-terminal domain enables rapid spider silk formation

Diversified Structural Basis of a Conserved Molecular Mechanism for pH-Dependent Dimerization in Spider Silk N-Terminal Domains

Protein stability curves

Apparent Debye-Huckel electrostatic effects in the folding of a simple, single domain protein

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

Crystal Structure of the Nephila clavipes Major Ampullate Spidroin 1A N-terminal Domain Reveals Plasticity at the Dimer Interface

P2888

s41598-017-16881-6

P304

16789

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P31

scholarly article

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10.1038/S41598-017-16881-6

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

P407

English

P433

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

P478

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2017-12-01T00:00:00Z

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29196631

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P932

5711802

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Conservation of folding and association within a family of spidroin N-terminal domains.

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P2860

P2860

Conservation of folding and association within a family of spidroin N-terminal domains.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P407

P433

P478

P577

P698

P932