Probing Protein Quinary Interactions by in-cell NMR.
Related Articles Probing Protein Quinary Interactions by in-cell NMR.
Biochemistry. 2015 Apr 20;
Authors: Majumder S, Xue J, DeMott CM, Reverdatto S, Burz DS, Shekhtman A
Abstract
Historically introduced by McConkey to explain the slow mutation rate of highly abundant proteins, protein weak (quinary) interactions are an emergent property of living cells. The protein complexes that result from quinary interactions are transient and thus difficult to study biochemically in vitro. Cross-correlated relaxation induced polarization transfer (CRIPT) based in-cell NMR allows the characterization of protein quinary interactions with atomic resolution inside live prokaryotic and eu-karyotic cells. We show that RNAs are an important component of protein quinary interactions. Protein quinary interactionss are unique to the target protein and affect physicochemical properties, protein ac-tivity, and interactions with drugs.
PMID: 25894651 [PubMed - as supplied by publisher]
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