The dimeric DNA binding domain of the human papillomavirus E2 protein folds through a monomeric intermediate which cannot be native-like (Q30176879)

9 June 2017

title

The dimeric DNA binding domain of the human papillomavirus E2 protein folds through a monomeric intermediate which cannot be native-like (English)

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9 June 2017

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Mok YK

1

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9 June 2017

Bycroft M

series ordinal

2

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9 June 2017

de Prat-Gay G

series ordinal

3

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9 June 2017

publication date

1 August 1996

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Nature structural biology

9 June 2017

published in

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9 June 2017

volume

3

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9 June 2017

issue

8

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9 June 2017

page(s)

711-717

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Crystal structure at 1.7 A of the bovine papillomavirus-1 E2 DNA-binding domain bound to its DNA target

9 June 2017

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Generation of a family of protein fragments for structure-folding studies. 2. Kinetics of association of the two chymotrypsin inhibitor-2 fragments

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Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.

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Energy coupling between DNA binding and subunit association is responsible for the specificity of DNA-Arc interaction

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31 March 2020

Identifiers

DOI

10.1038/NSB0896-711

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9 June 2017

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