Weak and Transient Protein Interactions Determined by Solid-State NMR

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 of a mechanism of regulation of E. coli DNA metabolism.


Published in:
Angewandte Chemie-International Edition, 55, 23, 6637-6640
Year:
2016
Publisher:
Weinheim, Wiley-Blackwell
ISSN:
1433-7851
Keywords:
Laboratories:




 Record created 2016-07-19, last modified 2018-09-13


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