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[ccp4bb] POST DOCTORAL POSITION IN STRUCTURAL ENZYMOLOGY AND INHIBITOR DESIGN

- Protein crystallography

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   - Crystallisation

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CCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999
Previous message:
Subject: model building and hardware (tangent)
From: "Bryan W {- dot -} Lepore" bryanlepore {- at -} MAIL {- dot -} UTEXAS {- dot -} EDU
Date: 2007-06-22
Next message:
Subject: Re: Ligand fitting in COOT and SHELX refinement
From: "George M {- dot -} Sheldrick" gsheldr {- at -} SHELX {- dot -} UNI-AC {- dot -} GWDG {- dot -} DE
Date: 2007-06-22


Subject: POST DOCTORAL POSITION IN STRUCTURAL ENZYMOLOGY AND INHIBITOR DESIGN
From: Steve Almo almo {- at -} MEDUSA {- dot -} BIOC {- dot -} AECOM {- dot -} YU {- dot -} EDU
Date: 2007-06-22

** POST DOCTORAL POSITION IN STRUCTURAL ENZYMOLOGY AND INHIBITOR DESIGN **

A post doctoral position is available immediately in the laboratories of
Vern Schramm and Steve Almo in the Department of Biochemistry at the
Albert Einstein College of Medicine. This program utilizes high resolution
crystallographic analysis and kinetic isotope effects to define the
fundamental chemical and physical determinants of enzymatic rate
enhancement, and to design highly specific transition state analogs with
affinities in the nM and pM ranges. These efforts are focused on the
enzymes involved in nucleotide metabolism in bacterial, fungal and
mammalian organisms and have produced a number of therapeutic leads that
are currently being utilized in animal studies and clinical trials for
malaria, T cell lymphoma and autoimmunity.

The successful applicant must have extensive experience in all aspects of
high resolution protein crystallography and a strong desire to complement
these skills with mechanistic enzymology and state-of-the-art transition
state analysis, with an overall goal of developing new therapeutic
approaches.

Representative publications describing this program include:
Fedorov, et al. (2001) “Transition state structure of purine nucleoside
phosphorylase and principles of atomic motion in enzymatic catalysis.
Biochemistry 40(4):853-60.

Lewandowicz, et al. (2003) Over-the-barrier transition state analogues and
crystal structure with Mycobacterium tuberculosis purine nucleoside
phosphorylase. Biochemistry 42(20):6057-66.

Singh, et al. (2004) Picomolar transition state analogue inhibitors of
human 5'-methylthioadenosine phosphorylase and X-ray structure with
MT-immucillin-A. Biochemistry 43(1):9-18.

Kim, et al. (2006) Structural and kinetic characterization of Escherichia
coli TadA, the wobble-specific tRNA deaminase. Biochemistry
45(20):6407-16.

Singh, et al. (2006) Structure and inhibition of a quorum sensing target
from Streptococcus pneumoniae. Biochemistry 45(43):12929-41.

Murkin, et al. (2007) Neighboring group participation in the transition
state of human purine nucleoside phosphorylase. Biochemistry
46(17):5038-49.


Albert Einstein provides an outstanding scientific environment that
includes considerable strengths in microbiology, immunology, cancer
biology, mechanistic enzymology, biophysics, computational biology and
structural genomics. Close proximity to the National Synchrotron Light
Source at Brookhaven National Laboratory ensures extensive and sustained
access to several bending magnet and insertion device beamlines. This
position affords the successful applicant with the opportunity to exploit
their expertise in structural biology within the context of a strong
biological program focused on inhibitor and therapeutic development.

Interested applicants should provide a CV and arrange for three letter of
reference to be sent directly to pcorr@medusa.bioc.aecom.yu.edu

CCP4bb navigation

CCP4bb <-- 1999 <-- November 1999 <-- 30 November 1999
Previous message:
Subject: model building and hardware (tangent)
From: "Bryan W {- dot -} Lepore" bryanlepore {- at -} MAIL {- dot -} UTEXAS {- dot -} EDU
Date: 2007-06-22
Next message:
Subject: Re: Ligand fitting in COOT and SHELX refinement
From: "George M {- dot -} Sheldrick" gsheldr {- at -} SHELX {- dot -} UNI-AC {- dot -} GWDG {- dot -} DE
Date: 2007-06-22



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