Dynamics of a family of cyan fluorescent proteins probed by incoherent neutron scattering.

ABSTRACT: Cyan fluorescent proteins (CFPs) are variants of green fluorescent proteins in which the central tyrosine of the chromophore has been replaced by a tryptophan. The increased bulk of the chromophore within a compact protein and the change in the positioning of atoms capable of hydrogen bonding have made it difficult to optimize their fluorescence properties, which took approximately 15 years between the availability of the first useable CFP, enhanced cyan fluorescent protein (ECFP), and that of a variant with almost perfect fluorescence efficiency, mTurquoise2. To understand the molecular bases of the progressive improvement in between these two CFPs, we have studied by incoherent neutron scattering the dynamics of five different variants exhibiting progressively increased fluorescence effi

SUBMITTER: Golub M 

PROVIDER: S-EPMC6451406 | biostudies-literature | 2019 Mar

REPOSITORIES: biostudies-literature