Postdoc Positions

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Postdoc Positions

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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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12-28-2010, 05:29 PM

nmrlearner

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Postdoc Positions

Postdoc Positions

Postdoctoral Opportunities: Structural Biology in Ubiquitination and Signaling

The Macromolecular NMR Section in the Structural Biophysics Laboratory has openings for postdoctoral fellows to work in the structural biology of protein complexes related to ubquitination, Arf proteins, and signaling via the STAT proteins. Our laboratory is involved in the application and development of state-of-the-art NMR spectroscopy, SAXS, and biophysics techniques to determine protein structures, investigate critical protein:protein interactions relevant to biological systems, analyze dynamic processes, and integrate these studies with molecular and cellular biology. We collaborate interactively with several biological, structural, and chemical groups in the Center for Cancer Research. Excellent NMR facilities (500-850 MHz), protein expression capabilities, and computational facilities are available.

Interested applicants should have a background in structural biology and experience in NMR spectroscopy. For examples of our work, please see Das, R., et al., Mol. Cell 34(6):674-685 (2009) and Das, R., et al., J. Mol. Biol. 376(3):705-720 (2008).

R. Andrew Byrd, Chief [byrdra@mail.nih.gov]
Structural Biophysics Laboratory
Center for Cancer Research
National Cancer Institute

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