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

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

doi:10.1002/anie.201210005

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

Angew Chem Int Ed Engl. 2013 Apr 22;52(17):4604-6. doi: 10.1002/anie.201210005. Epub 2013 Mar 20.

Authors

Jan Stanek¹, Saurabh Saxena, Leonhard Geist, Robert Konrat, Wiktor Koźmiński

Affiliation

¹ Faculty of Chemistry, University of Warsaw, Pasteura 1, 02093 Warsaw, Poland.

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

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Computer Simulation
Models, Molecular
Nuclear Magnetic Resonance, Biomolecular / methods*
Protein Conformation
Proteins / chemistry*

Substances

Proteins