Fluorescence enhancement of a ligand-activated fluorescent protein induced by collective noncovalent interactions.

ABSTRACT: Fluorescent proteins contain an internal chromophore constituted of amino acids or an external chromophore covalently bonded to the protein. To increase their fluorescence intensities, many research groups have attempted to mutate amino acids within or near the chromophore. Recently, a new type of fluorescent protein, called UnaG, in which the ligand binds to the protein through many noncovalent interactions was discovered. Later, a series of mutants of the UnaG protein were introduced, which include eUnaG with valine 2 mutated to leucine emitting significantly stronger fluorescence than the wild type and V2T mutant, in which valine 2 is mutated to threonine, emitting weaker fluorescence than the wild type. Interestingly, the single mutation sites of both eUnaG and V2T mutants are distant

SUBMITTER: Lee E 

PROVIDER: S-EPMC6249632 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature