Tracking multiple conformations occurring on angstrom-and-millisecond scales in single amino-acid-transporter molecules.

ABSTRACT: Most membrane protein molecules undergo conformational changes as they transition from one functional state to another one. An understanding of the mechanism underlying these changes requires the ability to resolve individual conformational states, whose changes often occur on millisecond and angstrom scales. Tracking such changes and acquiring a sufficiently large amount of data remain challenging. Here, we use the amino-acid transporter AdiC as an example to demonstrate the application of a high-resolution fluorescence-polarization-microscopy method in tracking multistate conformational changes of a membrane protein. We have successfully resolved four conformations of AdiC by monitoring the emission-polarization changes of a fluorophore label and quantified their probabilities in the pre

SUBMITTER: Zhou Y 

PROVIDER: S-EPMC9937647 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature