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Examining weak protein–protein interactions in start codon recognition via NMR spectroscopy
Author(s) -
Luna Rafael E.,
Akabayov Sabine R.,
Ziarek Joshua J.,
Wagner Gerhard
Publication year - 2014
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.12667
Subject(s) - nuclear magnetic resonance spectroscopy , ribosome , computational biology , start codon , biology , rna , chemistry , protein biosynthesis , biophysics , biochemistry , messenger rna , gene , stereochemistry
Weak protein–protein interactions are critical in numerous biological processes. Unfortunately, they are difficult to characterize due to the high concentrations required for the production and detection of the complex population. The inherent sensitivity of NMR spectroscopy to the chemical environment makes it an excellent tool to tackle this problem. NMR permits the exploration of interactions over a range of affinities, yielding essential insights into dynamic biological processes. The conversion of messanger RNA to protein is one such process that requires the coordinated association of many low‐affinity proteins. During start codon recognition, eukaryotic initiation factors assemble into high‐order complexes that bind messanger RNA and bring it to the ribosome for decoding. Many of the structures of the eukaryotic initiation factors have been determined; however, little is known regarding the weak binary complexes formed and their structure‐function mechanisms. Herein, we use start codon recognition as a model system to review the relevant NMR methods for the characterization of weak interactions and the development of small molecule inhibitors.