Abstract
Conformational fluctuations of a protein myoglobin in solution have been investigated by a time-resolved transient hole-burning experiment with a temporal resolution of ~ 10 ns over the temperature range of 180–300 K. The temperature dependence of the observed relaxation time τ r has been well fitted by the Vogel-Fulcher law. The solvent viscosity dependence of τ r has been also studied around room temperature.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: 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.