14. May 2018 - Laboratoire Léon Brillouin (CNRS - CEA)
Postdoctoral Position - Effect of pressure on t he structure and dynamics of C - phycocyanin
Postdoctoral Position - Effect of pressure on t he structure and dynamics of C - phycocyanin
14. May 2018 - Laboratoire Léon Brillouin (CNRS - CEA)
Postdoctoral Position - Effect of pressure on t he structure and dynamics of C - phycocyanin
Postdoctoral Position - Effect of pressure on t he structure and dynamics of C - phycocyanin
Employer
Laboratoire Léon Brillouin (CNRS - CEA)
Location

Saclay, France

Introduction

The Laboratoire Leon Brillouin (LLB) is a French Research Infrastructure jointly supported by CEA and CNRS (http://www-llb.cea.fr). The LLB operates both as a large-scale facility and a research institute. Neutrons are an invaluable technique to study a large variety of issues, including, for biological ones, protein folding/unfolding. The structure and the dynamics of proteins can be elucidated by small-angle neutron scattering (SANS) and inelastic/quasi elastic neutron scattering (INS/QENS), due to the characteristics time and length scales probed by these techniques (from ns to few hundreds and from fraction up to several hundreds nm). So far, only few experiments have addressed the structure and dynamics of biological materials upon application of high pressure (HP).

Job description

The LLB has a long experience in the development of HP cells for SANS and INS/QENS. In particular, a HP device has recently been developed for SANS experiments up to 6 kbars and has been applied to study the role of ligands and hydrophobic cavities in the unfolding of myoglobin, a small globular protein. The project is to study the effect of pressure on the structure and dynamics of Cphycocyanin (CPC), a hexameric light-harvesting pigment-protein complex. CPC unfolding occurs through the dissociation of the hexamer into monomers until the complete unfolding of its subunits. Structural and dynamical changes may occur not only at “high” pressure (3-6 kbars), where proteins generally unfold completely, but also at “lower” pressure (1.5-2 kbars), where the input of water in the hydrophobic cavities of proteins may provide intermediate folding conformations so far undetected.

Starting date & Duration: As early as October 2018 ; 18 months

Requested Profile

The successful candidate will be part of the “Soft Matter and Biophysics” scientific group. The position will allow the successful candidate to take advantage of the large in-house capabilities in biophysics research, neutron spectrometers, laboratory techniques, and access to the large scientific area around the “Plateau de Saclay”. Candidates are expected to have a PhD or similar in biophysics, biology, and/or biochemistry. Experimental experience in protein folding/unfolding would be highly appreciated. Experience with radiation techniques (X-ray or neutron scattering) would be advantageous.

Contact
Name

Sophie Combet

E-Mail
Website
How to Apply

Applications for this position should be sent by e-mail to and and include a C.V., the names of at least two references, and a cover letter summarizing current and future research initiatives.

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