Journal
BIOPHYSICAL JOURNAL
Volume 105, Issue 9, Pages 2157-2165Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2013.09.039
Keywords
-
Categories
Funding
- Grants-in-Aid for Scientific Research [25000013] Funding Source: KAKEN
Ask authors/readers for more resources
The bacterial flagellar filament is a very large macromolecular assembly of a single protein, flagellin. Various supercoiled states of the filament exist, which are formed by two structurally different conformations of flagellin in different ratios. We investigated the correlation between supercoiling of the protofilaments and molecular dynamics in the flagellar filament using quasielastic and elastic incoherent neutron scattering on the picosecond and nanosecond timescales. Thermal fluctuations in the straight L- and R-type filaments were measured and compared to the resting state of the wild-type filament. Amplitudes of motion on the picosecond timescale were found to be similar in the different conformational states. Mean-square displacements and protein resilience on the 0.1 ns timescale demonstrate that the L-type state is more flexible and less resilient than the R-type, whereas the wild-type state lies in between. Our results provide strong support that supercoiling of the protofilannents in the flagellar filament is determined by the strength of molecular forces in and between the flagellin subunits.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available