Postdoctoral Position at Cowburn Lab

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Postdoctoral Position at Cowburn Lab

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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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12-17-2010, 12:50 AM

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Postdoctoral Position at Cowburn Lab

Postdoctoral Position at Cowburn Lab

Postdoctoral Position at Cowburn Lab, Albert Einstein College of Medicine

An open postdoctoral position in structural biology is available for research on protein structure, dynamics, and function focusing on kinases and inteins.

Interested candidates should have a strong background in one or more of the following areas: multidimensional NMR, crystallography, protein expressions methods, and computer simulations of molecular structure and have completed their Ph.D.

Einstein provides a modern cross-disciplinary environment for research and education. NMR facilities include nine solution NMR spectrometers from 500 to 900 MHz equipped with cryogenic probes on site or at the New York Structural Biology Center. Extensive shared resources are available for protein production, crystallography, and high-performance computing.

The position is now available. Interested candidates should send their biographical sketch identifying three referees by email ( dc@cowburnlab.org ).

David Cowburn
Professor, Depts. of Biochemistry and of Physiology & Biophysics
Albert Einstein College of Medicine of Yeshiva University

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