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Default Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.

Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.

Related Articles Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer Data.

Angew Chem Int Ed Engl. 2016 Jan 28;

Authors: Gu Y, Hansen AL, Peng Y, Brüschweiler R

Abstract
Functional motions of (15) N-labeled proteins can be monitored by solution NMR spin relaxation experiments over a broad range of timescales. These experiments however typically take of the order of several days to a week per protein. Recently, NMR chemical exchange saturation transfer (CEST) experiments have emerged to probe slow millisecond motions complementing R1? and CPMG-type experiments. CEST also simultaneously reports on site-specific R1 and R2 parameters. It is shown here how CEST-derived R1 and R2 relaxation parameters can be measured within a few hours at an accuracy comparable to traditional relaxation experiments. Using a "lean" version of the model-free approach S(2) order parameters can be determined that match those from the standard model-free approach applied to (15) N R1 , R2 , and {(1) H}-(15) N NOE data. The new methodology, which is demonstrated for ubiquitin and arginine kinase (42 kDa), should serve as an effective screening tool of protein dynamics from picosecond-to-millisecond timescales.


PMID: 26821600 [PubMed - as supplied by publisher]



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