Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins. (Q36600090)

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2 February 2020

title

Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins (English)

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2 February 2020

2

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2 February 2020

Silvia Mangia

4

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2 February 2020

author name string

Nathaniel J Traaseth

1

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2 February 2020

Larry R Masterson

3

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2 February 2020

Michael Garwood

5

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2 February 2020

Shalom Michaeli

6

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2 February 2020

Burckhard Seelig

7

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2 February 2020

Gianluigi Veglia

8

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publication date

6 April 2012

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Journal of Magnetic Resonance

2 February 2020

published in

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volume

219

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page(s)

75-82

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Evidence for dynamics in proteins as a mechanism for ligand dissociation

2 February 2020

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A hierarchy of timescales in protein dynamics is linked to enzyme catalysis

30 September 2017

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Selection and evolution of enzymes from a partially randomized non-catalytic scaffold

30 September 2017

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Conformational entropy in molecular recognition by proteins

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28 June 2018

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20 September 2018

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20 September 2018

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20 September 2018

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Controlling the inhibition of the sarcoplasmic Ca2+-ATPase by tuning phospholamban structural dynamics.

20 September 2018

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20 September 2018

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20 September 2018

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20 September 2018

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20 September 2018

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20 September 2018

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12 December 2020

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Kinetics of Conformational Sampling in Ubiquitin

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Identifiers

DOI

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2 February 2020

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2 February 2020

PubMed publication ID

22621977

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