Abstract
Single molecule Forster resonance energy transfer (FRET) can provide both structural and dynamic information on proteins and has allowed us to map long-range intramolecular distances and reconfiguration dynamics in non-native states that are difficult to access with classical structural biology methods. Single molecule spectroscopy can also be used to investigate intrinsically disordered proteins and the folding and dynamics of proteins under more complex conditions, e.g. in the context of cellular factors, such as molecular chaperones.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
