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Default Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation.

Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation.

Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross-Correlated NMR Relaxation.

Angew Chem Int Ed Engl. 2013 Mar 20;

Authors: Stanek J, Saxena S, Geist L, Konrat R, Ko?mi?ski W

Abstract
Ab ultra-high-resolution NMR experiment for the measurement of intraresidue (1) H(i)-(15) N(i)-(13) C'(i) dipolar-chemical shift anisotropy relaxation interference is employed to extract information about local backbone geometries in intrinsically disordered proteins. The study of tumor suppressor BASP1 revealed a population shift of ?-turn geometries at low pH conditions and a compaction of the BASP1 structural ensemble.


PMID: 23520002 [PubMed - as supplied by publisher]



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