Thread: NMR paper Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
View Single Post
  #1  
Unread 08-25-2017, 04:11 AM
nmrlearner's Avatar
nmrlearner nmrlearner is offline
Senior Member
  
Join Date: Jan 2005
Posts: 23,207
Points: 193,617, Level: 100
Points: 193,617, Level: 100 Points: 193,617, Level: 100 Points: 193,617, Level: 100
Level up: 0%, 0 Points needed
Level up: 0% Level up: 0% Level up: 0%
Activity: 50.7%
Activity: 50.7% Activity: 50.7% Activity: 50.7%
Last Achievements
Award-Showcase
NMR Credits: 0
NMR Points: 0
Downloads: 0
Uploads: 0
Default Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.
Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.

Related Articles Analytical description of NMR relaxation highlights correlated dynamics in intrinsically disordered proteins.

Angew Chem Int Ed Engl. 2017 Aug 22;:

Authors: Blackledge M, Salvi N, Abyzov A

Abstract
The dynamic fluctuations of intrinsically disordered proteins (IDPs) define their function. Although experimental nuclear magnetic resonance (NMR) relaxation reveals the motional complexity of these highly flexible proteins, the absence of physical models describing IDP dynamics hinders their mechanistic interpretation. Combining molecular dynamics simulation and NMR, we introduce a framework in which distinct motions are attributed to local libration, backbone dihedral angle dynamics and longer-range tumbling of one or more peptide planes. This model provides unique insight into segmental organization of dynamics in IDPs and allows us to investigate the presence and extent of the correlated motions that are essential for function.


PMID: 28834051 [PubMed - as supplied by publisher]



More...
Reply With Quote

Did you find this post helpful? Yes | No