1. Atoms to Continuum:
Insights
into
the
molecular
mechanisms
of
myosin
7
regula4on
Glenn
Carrington1,
Sarah
Harris2,
Daniel
Read3,
Oliver
Harlen3,
Michelle
Peckham1
bs10g3c@leeds.ac.uk,
s.a.harris@leeds.ac.uk,
d.j.read@leeds.ac.uk,
o.j.harlen@leeds.ac.uk,
M.peckham@leeds.ac.uk
1
Faculty
of
Biological
Sciences,
University
of
Leeds,
LS2
9JT
2
School
of
Physics
and
Astronomy,
University
of
Leeds,
LS2
9JT
3
School
of
MathemaPcs,
University
of
Leeds,
LS2
9JT
Myosin 7a is a molecular motor that is auto-regulated by motor–tail interactions [1][2]. All atom molecular dynamics are used to study interactions
between residues at the nanometre and nanosecond scale. Fluctuating Finite Element Analysis (FFEA) is used to study fluctuating dynamics for the
whole molecule over longer timescales (microseconds), using coarse-grained approach [3]. I am using both to study myosin 7a behaviour.
What is FFEA?
FFEA treats proteins as visco-elastic continua
subject to deformation by thermal fluctuations.
PDB
EM
Density
Surface
Volume
Atomistic detail?
Interactions at the atomistic level allow myosin 7a to
adopt its regulated form.
Atomistic contributions to
overall protein dynamics:
I n t e r a c t i o n s a t t h e
atomistic level which
affect overall protein
dynamics need to be
investigated.
Coarse-graining
References:
[1] - Yang, Y. et al. (2009) Proc. Natl. Acad. Sci. U. S. A. 106, 4189–4194.
[2] - Umeki, N. et al. (2009) Proc. Natl. Acad. Sci. U. S. A. 106, 8483–8488.
[3] - Oliver, R. C. et al. (2013) J. Comput. Phys. 239, 147–165.
Conclusions and Future work
Myosin 7a couples large range conformational
changes with interactions at the atomistic level.
Future work will couple these two computational
regimes with experimental results.
Desolvation
Contributions
Electrostatic
Contributions Combining the nanoscale
and mesoscale:
Building the atomic
model: