Characterization of partially folded intermediates of papain in presence of cationic, anionic, and nonionic detergents at low pH

Biopolymers

Volumn 83, Issue 1, 2006, Pages 1-10

  Naeem, Aabgeena ^a   Fatima, Sadaf ^a   Khan, Rizwan Hasan ^a  

^a ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Anion induced state; Circular dichroism; Molten globule; Papain; Partially folded intermediate state

Indexed keywords

CONFORMATIONS; ENZYMES; FLUORESCENCE; HYDROPHOBICITY; PH EFFECTS;

ANION-INDUCED STATE; CIRCULAR DICHROISM; MOLTEN GLOBULE; PAPAIN; PARTIALLY FOLDED INTERMEDIATE STATE;

DETERGENTS;

1 ANILINO 8 SULFONIC ACID; CETRIMIDE; DETERGENT; DODECYL SULFATE SODIUM; PAPAIN; POLYSORBATE 20; SULFONIC ACID DERIVATIVE; TRYPTOPHAN; UNCLASSIFIED DRUG;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; PH; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE;

BIOPOLYMERS; CIRCULAR DICHROISM; DETERGENTS; HYDROGEN-ION CONCENTRATION; PAPAIN; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

EID: 33748363521     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20520     Document Type: Article

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