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Postdoc position

John Biggins BIGGINS%BROWNVM.bitnet at taunivm.tau.ac.il
Wed Apr 17 19:27:12 EST 1996


A post-doctoral research fellowship is available to study
protein-subunit interactions in the Photosystem l reaction center.
The investigations include:

  Elucidation of the domain of the FX cluster on the core heterodimer.

  The structure of the binding site for the PsaC subunit.

  The mechanism of the PsaC subunit/cofactor core interaction.

  The de novo design and synthesis of structures relevant to
   Photosystem 1 structure and electron transfer mechanisms.

The position is funded by the National Science Foundation and
can be filled immediately.  Candidates should be qualified in
biochemistry/molecular biology and preferably have expertise
in protein chemistry and molecular cloning.  Alternatively,
applicants from the physical/chemical sciences will be considered
if they have training in optical spectroscopy/signal processing/computer
technology etc and are interested in learning protein biochemistry
and molecular methods.

Recent references relevant to the project are:

Rodday, S., M., S-S Jun and Biggins, J. (1993)  Interaction of the
FAFB-containing subunit with the Photosystem l core heterodimer.
Photosyn. Research 36, 1-9.

Rodday, S., M., Schulz, R., McIntosh, L. and Biggins, J. (1994)
Structure-function studies on the interaction of PsaC with the
core heterodimer.  The site-directed change R561E in PsaB destabilizes
the subunit interaction in Synechocystis sp. PCC 6803.  Photosyn.
Research 42, 185-190.

Rodday, S., M., Webber, A., N., Bingham, S., E. and Biggins, J. (1995)
Evidence that the PsaB interhelical loop in the FX domain in
Photosystem l interacts with the subunit PsaC.  Site-directed
changes in PsaB destabilizes the subunit interaction in Chlamydomonas
reinhardtii.  Biochemistry 34, 6328-6334.

Candidates interested in the position should contact
 Dr. John Biggins
 Department of Molecular and Cell Biology & Biochemistry
 Brown University
 Providence, RI 02912    Tel: 401 863 2540
                         Fax: 401 863 1201


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