Detecting in-solution conformational changes in viral fusogens using tryptophan-induced fluorescence quenching.

ABSTRACT: Dynamic monitoring of protein conformational changes is necessary to fully understand many biological processes. For example, viral entry and membrane fusion require rearrangement of its viral glycoprotein. We present a step-by-step protocol for site-specific bimane labeling of the influenza-C fusogen to map proximity and conformational movements using tryptophan-induced fluorescence quenching. This protocol is adaptable for other proteins and for protein-protein interaction detection. For complete details on the use and execution of this protocol, please refer to Serrão et al., 2021.

SUBMITTER: Serrao VHB 

PROVIDER: S-EPMC8654978 | biostudies-literature |

REPOSITORIES: biostudies-literature