If space is provided, bulky modification on the rim of Azurin's β-barrel results in folded protein

FEBS Letters

Volumn 531, Issue 2, 2002, Pages 209-214

  Pozdnyakova, Irina ^a   Wittung Stafshede, Pernilla ^a  

^a Tulane University   (United States)

Author keywords

barrel stability; Azurin; Cysteine oxidation; Differential scanning calorimetry; Protein folding; Thermal denaturation

Indexed keywords

AZURIN; BACTERIAL PROTEIN; CYSTEINE; GLYCINE; HISTIDINE;

AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; HIGH TEMPERATURE; NONHUMAN; OXIDATION; PH; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN MODIFICATION; PROTEIN STRUCTURE; PSEUDOMONAS AERUGINOSA; THERMAL ANALYSIS; WILD TYPE;

APOPROTEINS; AZURIN; CALORIMETRY, DIFFERENTIAL SCANNING; CIRCULAR DICHROISM; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; MUTATION; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS AERUGINOSA; TEMPERATURE;

PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 0037032421     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(02)03505-6     Document Type: Article

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