Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins (Q34144556)

31 July 2017

title

Correlated dynamics of consecutive residues reveal transient and cooperative unfolding of secondary structure in proteins (English)

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31 July 2017

Patrik Lundström

1

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31 July 2017

Frans A A Mulder

series ordinal

2

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31 July 2017

Mikael Akke

series ordinal

3

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31 July 2017

language of work or name

English

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publication date

8 November 2005

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Proceedings of the National Academy of Sciences of the United States of America

31 July 2017

published in

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31 July 2017

volume

102

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31 July 2017

issue

47

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31 July 2017

page(s)

16984-16989

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Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR.

31 July 2017

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5 July 2018

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5 July 2018

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5 July 2018

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21 January 2018

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21 January 2018

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21 January 2018

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21 January 2018

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Probing multiple effects on 15N, 13C alpha, 13C beta, and 13C' chemical shifts in peptides using density functional theory

21 January 2018

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21 January 2018

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Differential multiple quantum relaxation caused by chemical exchange outside the fast exchange limit

21 January 2018

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12 December 2020

Probing slow backbone dynamics in proteins using TROSY-based experiments to detect cross-correlated time-modulation of isotropic chemical shifts

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12 December 2020

NMR characterization of the dynamics of biomacromolecules

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12 December 2020

Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations

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12 December 2020

Microsecond protein dynamics measured by 13Calpha rotating-frame spin relaxation

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12 December 2020

Differential multiple-quantum relaxation arising from cross-correlated time-modulation of isotropic chemical shifts

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12 December 2020

Identifiers

DOI

10.1073/PNAS.0504361102

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31 July 2017

0 references

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31 July 2017

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