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

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).

SUBMITTER: Kawale AA

PROVIDER: S-EPMC8567434 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature

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

Kawale Ashish A AA Burmann Björn M BM

STAR protocols 20211029 4

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 di ...[more]

PMID: 34761231

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