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

The comprehensive delineation of inherent dynamic motions embedded in pro-teins, which can be crucial for their functional repertoire, is often essential yet re-mains poorly understood in the majority of cases. In this protocol, we outline detailed descriptions of the necessary steps for employing solution NMR spec-troscopy for the in-depth amino acid level understanding of backbone dynamics of proteins. We describe the application of the protocol on the structurally anal-ogous 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).

Automated summary

This protocol outlines the detailed steps for using solution NMR spectroscopy to understand the backbone dynamics of proteins at the amino acid level. It also demonstrates the application of the protocol on structurally analogous Tudor domains with disparate functionalities.