(Q52541660)

3 May 2018

title

Dynamics of compact denatured states of glutaminyl-tRNA synthetase probed by bis-ANS binding kinetics. (English)

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3 May 2018

author name string

A Bhattacharyya

1

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3 May 2018

A K Mandal

2

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3 May 2018

R Banerjee

3

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3 May 2018

S Roy

4

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3 May 2018

publication date

1 October 2000

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3 May 2018

published in

Biophysical Chemistry

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3 May 2018

volume

87

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3 May 2018

issue

2-3

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3 May 2018

page(s)

201-212

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3 May 2018

Denatured states of proteins

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Aging of Tubulin Monomers Using 5,5'-Bis(8-anilino-1-naphthalenesulfonate) as a Probe

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A fluorescence spectroscopic study of glutaminyl-tRNA synthetase from Escherichia coli and its implications for the enzyme mechanism

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N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)colcemid, a probe for different classes of colchicine-binding site on tubulin

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The duplex-hairpin conformational transition of d(CGCGCGATCGCGCG) and d(CGCGCGTACGCGCG): a thermodynamic and kinetic study

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Proton Exchange and Basepair Kinetics of Yeast tRNAPhe and tRNAASP1

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A fluorescence spectroscopic study of substrate-induced conformational changes in glutaminyl-tRNA synthetase.

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Correlation between the amide proton exchange rates and the denaturation temperatures in globular proteins related to the basic pancreatic trypsin inhibitor

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Identifiers

DOI

1 reference

3 May 2018

1 reference

3 May 2018