Literature DB >> 29151213

Probing the Atomic Structure of Transient Protein Contacts by Paramagnetic Relaxation Enhancement Solution NMR.

Vincenzo Venditti1,2, Nicolas L Fawzi3.   

Abstract

Important biological processes, including enzyme catalysis, signaling, and protein folding, proceed through lowly populated (<5%) states that elude structural characterization by conventional techniques. Here, we describe the steps required for visualization of these sparsely populated conformations and transient protein-protein interactions using paramagnetic relaxation enhancement solution NMR. We describe experimental design, sample preparation, data acquisition and processing, and the basics of data analysis of structural ensembles.

Entities:  

Keywords:  Dark states; Encounter complex; Lowly populated states; NMR spectroscopy; Protein-protein interactions; Site-directed spin-labeling; Transient interactions

Mesh:

Year:  2018        PMID: 29151213      PMCID: PMC5823026          DOI: 10.1007/978-1-4939-7386-6_12

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  20 in total

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