Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York

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Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York

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NMR processing:

MDD

NMR assignment:

Backbone:

Side-chains:

NOEs:

Structure from NMR restraints:

Ab initio:

Fragment-based:

Rosetta-NMR (Robetta)

Template-based:

GeNMR

I-TASSER

Refinement:

Amber

Structure from chemical shifts:

Fragment-based:

Homology-based:

Torsion angles from chemical shifts:

Preditor

TALOS

Promega- Proline

Secondary structure from chemical shifts:

CSI (via RCI server)

TALOS

MICS caps, β-turns

d2D

PECAN

Flexibility from chemical shifts:

RCI

Interactions from chemical shifts:

HADDOCK

Chemical shifts re-referencing:

NMR model quality:

NOEs, other restraints:

Chemical shifts:

RDCs:

Pseudocontact shifts:

Protein geomtery:

SAVES2 or SAVES4

Quality Control Check

NMR spectrum prediction:

FANDAS

MestReS

V-NMR

Flexibility from structure:

Backbone S2

Methyl S2

B-factor

Molecular dynamics:

Gromacs

Amber

Antechamber

Chemical shifts prediction:

From structure:

Shiftx2

Sparta+

Camshift

CH3shift- Methyl

ArShift- Aromatic

ShiftS

Proshift

PPM

CheShift-2- Cα

From sequence:

Shifty

Camcoil

Poulsen_rc_CS

Disordered proteins:

MAXOCC

Format conversion & validation:

CCPN

From NMR-STAR 3.1

Validate NMR-STAR 3.1

NMR sample preparation:

Protein disorder:

DisMeta

Protein solubility:

Isotope labeling:

Solid-state NMR:

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08-21-2010, 05:17 AM

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Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York

Postdoctoral Position "Solution Dynamics of Protein Kinases" in New York

A postdoctoral position to study the solution dynamics and structure
of protein kinases is available on a NIH funded project (REF#:
HS-R-6453-10-08-S). Our group is interested in how static and dynamic
changes of protein structure affect the activity of protein kinases.
We combine X-ray crystallography, NMR and ligand binding kinetics with
collaborative molecular dynamic studies (See e.g. ref 1 and 2). Our
research group is located at Stony Brook University in a highly
interactive environment with the New York Structural Biology Center
and Brookhaven National Laboratory. Varian and Bruker NMR instruments
with 500-700 MHz field strenghts are available on site. As a member of
the New York Structural Biology Center, we have access to 800 MHz and
900 MHz instruments as well as a access to a large pool of NMR
expertise. The location of Stony Brook University within public
transport commuting distance to New York City and the north shore of
Long Island provide a convenient work-life balance and a family
friendly environment.
Interested candidates with a strong background in protein NMR should
email their CV and the names of three references to Markus Seeliger
(markus.seeliger@gmail.com).

1.) Shan, Y., Seeliger, M.A., et al. A conserved
protonation-dependent switch controls drug binding in the Abl kinase.
Proc Natl Acad Sci U S A, 2009. 106(1): p. 139-44.

2.) Seeliger, M.A., et al., Equally potent inhibition of c-Src and Abl
by compounds that recognize inactive kinase conformations. Cancer Res,
2009. 69(6): p. 2384-92.

************************************************** *****
Markus Seelige
Assistant Professor
Department of Pharmacological Sciences
Stony Brook University Medical School, BST 7-125
Stony Brook, NY 11794-8651
phone: (631) 444-3558 fax: (631) 444-9749
http://www.pharm.stonybrook.edu/seeliger
************************************************** *****

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