Probing Local Backbone Geometries in Intrinsically Disordered Proteins by Cross‐Correlated NMR Relaxation | Zendy

Stanek Jan | Zendy; Saxena Saurabh | Zendy; Geist Leonhard | Zendy; Konrat Robert | Zendy; Koźmiński Wiktor | Zendy

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

Author(s) -

Stanek Jan,

Saxena Saurabh,

Geist Leonhard,

Konrat Robert,

Koźmiński Wiktor

Publication year - 2013

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201210005

Subject(s) - intrinsically disordered proteins , relaxation (psychology) , chemical physics , anisotropy , population , chemistry , dipole , nuclear magnetic resonance , materials science , crystallography , physics , optics , organic chemistry , psychology , social psychology , demography , sociology

An 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 β‐turn geometries at low pH conditions and a compaction of the BASP1 structural ensemble.

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