Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified β-lactoglobulin: Relevance towards anti-HIV binding

Journal of Photochemistry and Photobiology B: Biology

Volumn 102, Issue 1, 2011, Pages 1-10

  Chakraborty, Jishnu ^a   Das, Niloy ^a   Halder, Umesh Chandra ^a  

^a JADAVPUR UNIVERSITY   (India)

Author keywords

Lactoglobulin; Acetylation; ANS; Fluorescence resonance energy transfer; Lifetime decay; Succinylation

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACETIC ACID DERIVATIVE; BETA LACTOGLOBULIN; LYSINE; TRYPTOPHAN DERIVATIVE;

ACETYLATION; ARTICLE; BIOTRANSFORMATION; CHEMICAL MODIFICATION; ENERGY TRANSFER; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN IMMUNODEFICIENCY VIRUS; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL;

ACETYLATION; ANILINO NAPHTHALENESULFONATES; ANIMALS; ANTI-HIV AGENTS; CATTLE; FLUORESCENCE RESONANCE ENERGY TRANSFER; HIV; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; LACTOGLOBULINS; LIGANDS; LYSINE; PROTEIN BINDING; PROTEIN UNFOLDING; STATIC ELECTRICITY; SUCCINIC ACID;

BOVINAE;

EID: 78650907815     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jphotobiol.2010.08.010     Document Type: Article

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