Mechanism and bottlenecks in strand photodissociation of split green fluorescent proteins (GFPs).

ABSTRACT: Split GFPs have been widely applied for monitoring protein-protein interactions by expressing GFPs as two or more constituent parts linked to separate proteins that only fluoresce on complementing with one another. Although this complementation is typically irreversible, it has been shown previously that light accelerates dissociation of a noncovalently attached β-strand from a circularly permuted split GFP, allowing the interaction to be reversible. Reversible complementation is desirable, but photodissociation has too low of an efficiency (quantum yield <1%) to be useful as an optogenetic tool. Understanding the physical origins of this low efficiency can provide strategies to improve it. We elucidated the mechanism of strand photodissociation by measuring the dependence of its rate on l

SUBMITTER: Lin CY 

PROVIDER: S-EPMC5358378 | biostudies-literature | 2017 Mar

REPOSITORIES: biostudies-literature