| Literature DB >> 29151213 |
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