Organization and dynamics of tryptophan residues in tetrameric and monomeric soybean agglutinin: Studies by steady-state and time-resolved fluorescence, phosphorescence and chemical modification

Biochimie

Volumn 91, Issue 7, 2009, Pages 857-867

  Molla, Anisur R ^a   Maity, Shyam S ^a   Ghosh, Sanjib ^a   Mandal, Dipak K ^a  

^a PRESIDENCY UNIVERSITY   (India)

Author keywords

Fluorescence; Folding and association; Oligomeric protein; Phosphorescence; Soybean agglutinin; Tryptophan modification

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACRYLAMIDE; MONOMER; N BROMOSUCCINIMIDE; OLIGOMER; SOYBEAN AGGLUTININ; TETRAMER; TRYPTOPHAN DERIVATIVE;

ANISOTROPY; ARTICLE; BINDING AFFINITY; CHEMICAL MODIFICATION; CONTROLLED STUDY; FLUORESCENCE ANALYSIS; HYDROPHOBICITY; MOLECULAR DYNAMICS; OXIDATION; PHOSPHORESCENCE; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STRUCTURE; STEADY STATE; TIME;

ANILINO NAPHTHALENESULFONATES; BROMOSUCCINIMIDE; FLUORESCENCE POLARIZATION; OXIDATION-REDUCTION; PLANT LECTINS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; SOYBEAN PROTEINS; TRYPTOPHAN;

GLYCINE MAX;

EID: 67349237729     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.04.006     Document Type: Article

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