Murine norovirus protein NS1/2 aspartate to glutamate mutation, sufficient for persistence, reorients side chain of surface exposed tryptophan within a novel structured domain

Proteins: Structure, Function and Bioinformatics

Volumn 82, Issue 7, 2014, Pages 1200-1209

  Borin, Brendan N ^a   Tang, Wei ^b   Nice, Timothy J ^b   Mccune, Broc T ^b   Virgin, Herbert W ^b   Krezel, Andrzej M ^b  

^a NMR Accelerator   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Helix strand helix; MNV; PEST motif; Polyprotein; Protein NMR; Side chain rotamers

Indexed keywords

ASPARTIC ACID; GLUTAMIC ACID; INDOLE; NONSTRUCTURAL PROTEIN 1; NONSTRUCTURAL PROTEIN 2; POLYPEPTIDE; TRYPTOPHAN; VIRUS PROTEIN; AMINO ACID; VIRAL PROTEIN;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; CIRCULAR DICHROISM; HETERONUCLEAR NUCLEAR MAGNETIC RESONANCE; MOLECULAR RECOGNITION; MOUSE; MURINAE; NONHUMAN; NOROVIRUS; NUCLEAR MAGNETIC RESONANCE; NUCLEAR OVERHAUSER EFFECT; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SURFACE PROPERTY; VIRUS MUTATION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; MOLECULAR GENETICS; MUTATION;

AMINO ACID SEQUENCE; AMINO ACIDS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NOROVIRUS; PROTEIN CONFORMATION; VIRAL NONSTRUCTURAL PROTEINS;

EID: 84902108996     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24484     Document Type: Article

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