Atomic mutations at the single tryptophan residue of human recombinant annexin V: Effects on structure, stability, and activity

Biochemistry

Volumn 38, Issue 33, 1999, Pages 10649-10659

  Minks, Caroline ^a   Huber, Robert ^a   Moroder, Luis ^a   Budisa, Nediljko ^a  

^a MAX PLANCK INSTITUTE OF BIOCHEMISTRY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

LIPOCORTIN 5; TRYPTOPHAN;

ARTICLE; COVALENT BOND; HUMAN; HUMAN CELL; ION EXCHANGE; MUTATION; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; X RAY CRYSTALLOGRAPHY;

ANNEXIN A5; CALCIUM; CIRCULAR DICHROISM; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; HEAT; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PRESSURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; SOLUTIONS; SPECTROMETRY, FLUORESCENCE; STRUCTURE-ACTIVITY RELATIONSHIP; TRYPTOPHAN;

EID: 0033578445     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi990580g     Document Type: Article

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