Prion protein mPrP[F175A](121-231): Structure and stability in solution

Journal of Molecular Biology

Volumn 423, Issue 4, 2012, Pages 496-502

  Christen, Barbara ^a   Hornemann, Simone ^a   Damberger, Fred F ^a   Wüthrich, Kurt ^a,b  

^a ETH ZURICH   (Switzerland)

^b SCRIPPS RESEARCH INSTITUTE   (United States)

Author keywords

CD spectroscopy; NMR structure; protein denaturation; transmissible spongiform encephalopathies; variant mouse prion protein

Indexed keywords

ALANINE; HELIX LOOP HELIX PROTEIN; PHENYLALANINE; PHENYLALANINE 175; PRION PROTEIN; PRION PROTEIN[121-231]; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; LOW TEMPERATURE; MOUSE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; PROTEIN UNFOLDING; TEMPERATURE; THERMAL STIMULATION;

MAMMALIA;

EID: 84867245306     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2012.08.011     Document Type: Article

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