Weak and Transient Protein Interactions Determined by Solid-State NMR

Authors

Hugh R W Dannatt, University of Lyon
Michelle Felletti, University of Lyon
S Jehle, University of Lyon
Yao Wang, University of Wollongong
Lyndon Emsley, University of Lyon, Ecole Polytechnique Federale de Lausanne
Nicholas E. Dixon, University of WollongongFollow
A Lesage, University of Lyon
Guido Pintacuda, University of LyonFollow

RIS ID

114318

Publication Details

Dannatt, H. R W., Felletti, M., Jehle, S., Wang, Y., Emsley, L., Dixon, N. E., Lesage, A. & Pintacuda, G. (2016). Weak and Transient Protein Interactions Determined by Solid-State NMR. Angewandte Chemie International Edition, 55 6638-6641.

Abstract

Despite their roles in controlling many cellular processes, weak and transient interactions between large structured macromolecules and disordered protein segments cannot currently be characterized at atomic resolution by Xray crystallography or solution NMR. Solid-state NMR does not suffer from the molecular size limitations affecting solution NMR, and it can be applied to molecules in different aggregation states, including non-crystalline precipitates and sediments. A solid-state NMR approach based on high magnetic fields, fast magic-angle sample spinning, and deuteration provides chemical-shift and relaxation mapping that enabled the characterization of the structure and dynamics of the transient association between two regions in an 80 kDa protein assembly. This led to direct verification ofamechanism of regulation of E. coli DNA metabolism.

Grant Number

ARC/DP0984797