Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies (Q74418259)

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10 November 2019

title

Backbone dynamics of the natively unfolded pro-peptide of subtilisin by heteronuclear NMR relaxation studies (English)

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10 November 2019

author name string

A V Buevich

1

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10 November 2019

U P Shinde

2

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10 November 2019

M Inouye

3

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10 November 2019

J Baum

4

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10 November 2019

publication date

1 July 2001

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Journal of Biomolecular NMR

10 November 2019

published in

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10 November 2019

volume

20

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10 November 2019

page(s)

233-249

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10 November 2019

issue

3

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https://scigraph.springernature.com/pub.10.1023/a:1011243116136

10 November 2019

exact match

0 references

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Backbone dynamics of a highly disordered 131 residue fragment of staphylococcal nuclease

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Structural and Dynamical Characterization of a Biologically Active Unfolded Fibronectin-Binding Protein fromStaphylococcusaureus†

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1H NMR Analysis of the Partly-folded Non-native Two-disulphide Intermediates (30-51,5-14) and (30-51,5-38) in the Folding Pathway of Bovine Pancreatic Trypsin Inhibitor

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