Mechanistic Insights into Water–Protein Interactions of Filamentous Bacteriophage
作者： Rudra N. Purusottam , Ratan K. Rai , Neeraj Sinha
DOI: 10.1021/JP310921N
关键词: Molecule 、 Protein subunit 、 Protein–protein interaction 、 Heteronuclear molecule 、 Nuclear magnetic resonance spectroscopy 、 Crystallography 、 Magic angle spinning 、 Supramolecular assembly 、 Filamentous bacteriophage 、 Chemistry
摘要: Water plays a major structural and functional role around proteins. In an attempt to explore this mechanistic aspect of proteins, we present site-specific interaction hydration water with the coat protein subunit filamentous virus Pf1 by magic angle spinning (MAS) solid-state NMR. The surrounding 36 MDa virion is investigated in uniformly 13 C, 15 N isotopically labeled; polyethylene glycol precipitated fully hydrated samples nuclear magnetic resonance spectroscopy. Dipolar edited two-dimensional (2D) 1 H� heteronuclear correlation (HETCOR) experiments lead unambiguous assignments cross-peaks originating exclusively from H resonances molecules correlating amide nitrogen. An enhanced resolved chemical shift dimension these also precludes need perdeuteration. We report seven residues spanning 40-residue continuous α-helical conformation assembly interacting water. It shows highly inner core inside viral assembly. results obtained suggest first evidence water-mediated interface cluster formed at site Arg44 single-stranded DNA genome phage supramolecular
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