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Date: Thu Aug 28 15:46:15 2008
Subject: 08.08.18 Postdoctoral Research Associates in Protein/Ligands Interactions and Dynamics
Postdoctoral Research Associates in Protein/Ligands
Interactions and Dynamics
Biosciences Division Biological and Environmental Sciences Directorate
Oak Ridge National Laboratory Oak Ridge, Tennessee
ORNL08-114-BESD
Project Description: The Biosciences Division at the Oak Ridge National
Laboratory is seeking to fill a postdoctoral research position in
protein/ligands interactions and dynamics, coupled with experimental
neutron scattering experiments and solution NMR.
The dynamics of protein play a key role in their function, and in
particular in their capacity to bind biologically important ligands.
The research here will provide a framework for understanding the
energetics and dynamics of protein/ligand interactions, combining
high-performance simulation with experiments on a next-generation
neutron source, the new Spallation Neutron Source at Oak Ridge National
Laboratory. This project will be done in collaboration with research
groups at the University of Tennessee, Knoxville, for molecular biology
and solution NMR experiments.
Specifically, we aim to (i) Perform molecular modeling simulations to
investigate the dynamics and thermodynamics of protein/ligand interactions,
in particular the dynamics of opening/closing of substrate access channels
and product release channels. (ii) Perform neutron scattering experiments
aimed at identifying the protein residues that undergo dynamical change
during ligand access/release. (iii) Interface with collaborators for
specific labeling experiments and solution NMR experiments.
Several crystal structures exist for apo- and bound- species of proteins
and protein/ligand complexes. In several cases, the apo- and bound- species
do not exhibit major changes outside the very binding site domain. However,
transient structural changes are needed to allow the ligand to move from
the cytoplasmic environment to the inside of the protein. Molecular
simulations of the ligand entry and exit pathways can be performed to
identify protein domains involved and the corresponding dynamics.
Neutron spectroscopy experiments can be used to investigate and verify
that residues suggested by the simulation as important are indeed
experiencing modified structural environment and dynamics upon ligand
binding. Solution NMR will provide complementary results and will be
included in the design of the simulations.
Qualifications: A Ph.D. in chemistry, physics, biophysics or closely
related field. Applicants cannot have received the most recent degree
more than five years prior to the date of application appointment
and must complete all degree requirements before starting their appointment.
Technical Information:
For additional information contact:
Jerome Baudry, Ph.D.
Assistant Professor, University of Tennessee, Knoxville.
Department of Biochemistry & Cellular and Molecular Biology.
UT/ORNL Center for Molecular Biophysics
Building 6011, Oak Ridge National Laboratory Oak Ridge, Tennessee 37830, USA
TEL: (865) 576 0930
baudryjy**ornl.gov
http://cmb.ornl.gov/group/baudry
How to Apply:
Qualified applicants must apply online at
https://www2.orau.gov/ORNL_POST/.
All applicants will need to register before they can begin the online
application. For complete instructions, on how to apply, please see the
instructions at
http://www.orau.gov/orise/edu/ornl/ornl-pdpm/application.htm.
When applying for this position, please reference the position title and
number. This appointment is offered through the ORNL Postgraduate
Research Participation Program and is administered by the Oak Ridge
Institute for Science and Education (ORISE). The position is open to
citizens or legal permanent residents of the US without regard to race,
color, age, religion, sex, national origin, physical or mental disability,
or status as a Vietnam-era veteran or disabled veteran.
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