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






4 Functional Relationships(s)
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1 Unfolding diminishes fluorescence resonance energy transfer (FRET) of lysine modified beta-lactoglobulin: Relevance towards anti-HIV binding. Lysine 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. Lysine beta-lactoglobulin Bos taurus
3 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. Lysine beta-lactoglobulin Bos taurus
4 Lysine residues of beta-lg were modified by acetylation and succinylation. Lysine beta-lactoglobulin Bos taurus