| Autor: |
Labe Black, J.B. Alexander Ross |
| Rok vydání: |
2018 |
| Předmět: |
|
| Zdroj: |
Reviews in Fluorescence 2017 ISBN: 9783030015688 |
| DOI: |
10.1007/978-3-030-01569-5_12 |
| Popis: |
Time-resolved fluorescence anisotropy (TRFA) is a well-established method for studying molecular dynamics that occur on a timescale from picoseconds to tens of nanoseconds. This method can be used to investigate ligand-dependent changes in the local motions of regions of interest (for example loop dynamics) in proteins and protein assemblies. TRFA data are generally fitted to models based on sums of exponentials, and cross-correlation between fitting parameters can significantly affect the accuracy and precision of the recovered parameters that are associated with local and global motions. Here, fluorescence correlation spectroscopy (FCS) data is used to obtain an independent measure of the whole molecule motion and calculate the mean rotational correlation time, which is then used to reduce cross-correlation with the TRFA parameters associated with the local motions. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
|
