Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins

Ashish A Kawale; Björn M Burmann

doi:10.1016/j.xpro.2021.100919

Characterization of backbone dynamics using solution NMR spectroscopy to discern the functional plasticity of structurally analogous proteins

STAR Protoc. 2021 Oct 29;2(4):100919. doi: 10.1016/j.xpro.2021.100919. eCollection 2021 Dec 17.

Authors

Ashish A Kawale^{1

2}, Björn M Burmann^{1

2}

Affiliations

¹ Wallenberg Centre for Molecular and Translational Medicine, University of Gothenburg, 405 30 Gothenburg, Sweden.
² Department of Chemistry and Molecular Biology, University of Gothenburg, 405 30 Gothenburg, Sweden.

Abstract

The comprehensive delineation of inherent dynamic motions embedded in proteins, which can be crucial for their functional repertoire, is often essential yet remains poorly understood in the majority of cases. In this protocol, we outline detailed descriptions of the necessary steps for employing solution NMR spectroscopy for the in-depth amino acid level understanding of backbone dynamics of proteins. We describe the application of the protocol on the structurally analogous Tudor domains with disparate functionalities as a model system. For complete details on the use and execution of this protocol, please refer to Kawale and Burmann (2021).

Keywords: Biophysics; NMR; Protein Biochemistry; Structural Biology.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Magnetic Resonance Spectroscopy / methods*
Molecular Dynamics Simulation
Protein Conformation
Proteins / chemistry*

Substances

Proteins

Grants and funding

P41 GM111135/GM/NIGMS NIH HHS/United States