Abstract
Time-resolved transient hole-burning (TRTHB) spectroscopy is quite effective to elucidate the conformational fluctuation dynamics of protein in ns-ms time regime, which has not been investigated intensively so far. It has also great importance for the understanding of the molecular-level mechanism of protein functioning. TRTHB study on Zn-substituted myoglobin has clarified its highly non-exponential fluctuation dynamics. The time scale of the observed fluctuation is distributed over very wide range from ns to μs. The results underscore the utility of the present method to characterize conformational dynamics of protein.
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.
