The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening (Q46067451)

19 December 2017

title

The N-terminal domains of spider silk proteins assemble ultrafast and protected from charge screening (English)

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19 December 2017

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Simone Schwarze

1

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19 December 2017

Fabian U Zwettler

series ordinal

2

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19 December 2017

Christopher M Johnson

series ordinal

3

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19 December 2017

Hannes Neuweiler

series ordinal

4

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19 December 2017

language of work or name

English

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publication date

1 January 2013

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19 December 2017

published in

Nature Communications

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19 December 2017

volume

4

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19 December 2017

page(s)

2815

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19 December 2017

Liquid crystalline spinning of spider silk

cites work

1 reference

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Review the role of terminal domains during storage and assembly of spider silk proteins

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

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

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pH-Dependent Dimerization and Salt-Dependent Stabilization of the N-terminal Domain of Spider Dragline Silk-Implications for Fiber Formation

21 January 2018

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Spidroin N-terminal domain promotes a pH-dependent association of silk proteins during self-assembly

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Profluorescent protease substrates: intramolecular dimers described by the exciton model

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

21 January 2018

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Fundamental aspects of protein-protein association kinetics

21 January 2018

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The kinetics of PDZ domain-ligand interactions and implications for the binding mechanism

21 January 2018

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Protein ionizable groups: pK values and their contribution to protein stability and solubility

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Unraveling A Trap-and-Trigger Mechanism in the pH-Sensitive Self-Assembly of Spider Silk Proteins

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Downhill versus barrier-limited folding of BBL 1: energetic and structural perturbation effects upon protonation of a histidine of unusually low pKa.

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Effect of sodium chloride on the structure and stability of spider silk's N-terminal protein domain

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Rational design of faster associating and tighter binding protein complexes.

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Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'.

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On the calculation of electrostatic interactions in proteins.

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Electrostatic screening of charge and dipole interactions with the helix backbone

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Simulation of flow in the silk gland

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Consequences of forced silking

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Changes in element composition along the spinning duct in a Nephila spider.

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A pH-dependent dimer lock in spider silk protein

21 January 2018

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Prediction of Protein-Protein Association Rates from a Transition-State Theory

21 January 2018

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Silk production in a spider involves acid bath treatment

21 January 2018

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inferred from DOI database lookup

7 January 2021

based on heuristic

Dimer formation of organic fluorophores reports on biomolecular dynamics under denaturing conditions

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS3815

inferred from DOI database lookup

7 January 2021

based on heuristic

Rapid, electrostatically assisted association of proteins

1 reference

https://api.crossref.org/works/10.1038%2FNCOMMS3815

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1038/NCOMMS3815

1 reference

19 December 2017

ADS bibcode

2013NatCo...4.2815S

0 references

1 reference

19 December 2017