Role of disulfide bonds for the structure and folding of proguanylin

Biochemistry

Volumn 43, Issue 31, 2004, Pages 10050-10057

  Lauber, Thomas ^a   Schulz, Axel ^b   Rösch, Paul ^a   Marx, Ute C ^a  

^a UNIVERSITY OF BAYREUTH   (Germany)

^b IPF PHARMACEUTICALS GMBH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; HYDROPHOBICITY; MOLECULAR STRUCTURE; POLYPEPTIDES; PROTEINS;

DISULFIDE BONDS; HELICAL CORE STRUCTURES; HYDROPHOBIC CORE; PROGUANYLIN;

HORMONES;

GUANYLIN; HORMONE PRECURSOR; PROGUANYLIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; DELETION MUTANT; DISULFIDE BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; PROTEIN TERTIARY STRUCTURE; STRUCTURE ANALYSIS; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; CYSTEINE; DISULFIDES; GASTROINTESTINAL HORMONES; HUMANS; MOLECULAR SEQUENCE DATA; NATRIURETIC PEPTIDES; NITROGEN ISOTOPES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEIN SORTING SIGNALS; RECOMBINANT PROTEINS; SERINE; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 3543112006     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049667e     Document Type: Article

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