Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation

Nicola Salvi; Anton Abyzov; Martin Blackledge

doi:10.1021/acs.jpclett.6b00885

Journal Articles Journal of Physical Chemistry Letters Year : 2016

Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation

(1) , (1) , (1)

1

Nicola Salvi

Function : Author
PersonId : 764706
ORCID : 0000-0003-1515-6908
IdRef : 184453941

Institut de biologie structurale

Anton Abyzov

Function : Author

Institut de biologie structurale

Martin Blackledge

Function : Author
PersonId : 760553
ORCID : 0000-0003-0935-721X
IdRef : 095872086

Institut de biologie structurale

Domains

Life Sciences [q-bio] Biochemistry, Molecular Biology Structural Biology [q-bio.BM]

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https://hal.univ-grenoble-alpes.fr/hal-01396234

Submitted on : Monday, November 14, 2016-11:08:36 AM

Last modification on : Monday, March 13, 2023-10:56:15 AM

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hal-01396234 , version 1 (14-11-2016)

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HAL Id : hal-01396234 , version 1
DOI : 10.1021/acs.jpclett.6b00885
PUBMED : 27300592

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Nicola Salvi, Anton Abyzov, Martin Blackledge. Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation. Journal of Physical Chemistry Letters, 2016, 7 (13), pp.2483 - 2489. ⟨10.1021/acs.jpclett.6b00885⟩. ⟨hal-01396234⟩

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Multi-Timescale Dynamics in Intrinsically Disordered Proteins from NMR Relaxation and Molecular Simulation

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