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

Pub. Date : 2011 Jan 10

PMID : 20875748






3 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 In this article, interactions between lysine modified bovine beta-lactoglobulin (beta-lg) and a hydrophobic fluorescence probe, 1-anilinonapthalene-8-sulfonate (ANS), have been studied with the help of fluorescence resonance energy transfer (FRET) process. 1-anilino-8-naphthalenesulfonate beta-lactoglobulin Bos taurus
2 In this article, interactions between lysine modified bovine beta-lactoglobulin (beta-lg) and a hydrophobic fluorescence probe, 1-anilinonapthalene-8-sulfonate (ANS), have been studied with the help of fluorescence resonance energy transfer (FRET) process. 1-anilino-8-naphthalenesulfonate beta-lactoglobulin Bos taurus
3 Furthermore, time resolved studies showed that in the derivatives, hydrophobic cavities of beta-lg were collapsed so that ANS failed to recognize the deep interior pockets leading to the loss of longer lifetime component. 1-anilino-8-naphthalenesulfonate beta-lactoglobulin Bos taurus