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 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 sol...

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Bibliographic Details
Published in:STAR protocols 2021-12, Vol.2 (4), p.100919-100919, Article 100919
Main Authors: Kawale, Ashish A., Burmann, Björn M.
Format: Article
Language:English
Subjects:
Biophysics
Clinical Medicine
Klinisk medicin
Magnetic Resonance Spectroscopy - methods
Molecular Dynamics Simulation
NMR
Protein Biochemistry
Protein Conformation
Proteins - chemistry
Protocol
Structural Biology
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Summary: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). [Display omitted] •Backbone dynamics characterization of Tudor domains by solution NMR spectroscopy•Step-by-step setup and analysis scheme for 15N NMR relaxation experiments•Practical guide for discerning dynamics of structurally analogous proteins•Protocol applicable for small-to-medium sized proteins and protein-ligand complexes 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.
ISSN:2666-1667
2666-1667
DOI:10.1016/j.xpro.2021.100919