Distance mapping in proteins using fluorescence spectroscopy: the tryptophan-induced quenching (TrIQ) method.

ABSTRACT: Studying the interplay between protein structure and function remains a daunting task. Especially lacking are methods for measuring structural changes in real time. Here we report our most recent improvements to a method that can be used to address such challenges. This method, which we now call tryptophan-induced quenching (TrIQ), provides a straightforward, sensitive, and inexpensive way to address questions of conformational dynamics and short-range protein interactions. Importantly, TrIQ only occurs over relatively short distances (∼5-15 Å), making it complementary to traditional fluorescence resonance energy transfer (FRET) methods that occur over distances too large for precise studies of protein structure. As implied in the name, TrIQ measures the efficient quenching induced in some

SUBMITTER: Mansoor SE 

PROVIDER: S-EPMC3938424 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature