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Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation.

ABSTRACT: 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 ?-turn geometries at low pH conditions and a compaction of the BASP1 structural ensemble.

SUBMITTER: Stanek J

PROVIDER: S-EPMC3659411 | biostudies-literature | 2013 Apr

REPOSITORIES: biostudies-literature

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Probing local backbone geometries in intrinsically disordered proteins by cross-correlated NMR relaxation.

Stanek Jan J Saxena Saurabh S Geist Leonhard L Konrat Robert R Koźmiński Wiktor W

Angewandte Chemie (International ed. in English) 20130320 17

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. ...[more]

PMID: 23520002

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

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