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NMR processing:
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NMR assignment:
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MARS
UNIO Match
PINE
Side-chains:
UNIO ATNOS-Ascan
NOEs:
UNIO ATNOS-Candid
UNIO Candid
ASDP
Structure from NMR restraints:
Ab initio:
GeNMR
Cyana
XPLOR-NIH
ASDP
UNIO ATNOS-Candid
UNIO Candid
Fragment-based:
BMRB CS-Rosetta
Rosetta-NMR (Robetta)
Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
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:
Shiftcor
UNIO Shiftinspector
LACS
CheckShift
RefDB
NMR model quality:
NOEs, other restraints:
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RPF scores
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Chemical shifts:
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Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
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Protein geomtery:
Resolution-by-Proxy
PROSESS
What-If
iCing
PSVS
MolProbity
SAVES2 or SAVES4
Vadar
Prosa
ProQ
MetaMQAPII
PSQS
Eval123D
STAN
Ramachandran Plot
Rampage
ERRAT
Verify_3D
Harmony
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:
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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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
sedNMR


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Old 12-06-2007, 08:01 AM
mww mww is offline
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Default Postdoctoral position in protein dynamics

A two year postdoctoral position in protein NMR is open at the department of chemistry, University of Umeå, Sweden. The research in our group is focused on understanding the cooperativity of conformational change and protein folding. To this end we have established suitable model systems. The direction of research for the open position will depend on the interests of the candidate.

We are using state of the art NMR experiments, such as relaxation dispersion, to quantify conformational exchange dynamics. In addition we use ultrafast SOFAST-HMQC experiments to measure hydrogen exchange which is an extremely useful tool in many cases. Protein engineering is an integral part of all our research projects. Structure determination is pursued when necessary.

The department harbors two high field Bruker NMR spectrometers, one 500 MHz instrument equipped with a warm probe and one 600 MHz instrument equipped with a cold triple resonance probe. In addition, we have access to both 800 and 900 Varian spectrometers located at the Swedish NMR centre in Gothenburg; these instruments can be operated remotely from our lab.

We are seeking candidates with documented skills in solution state protein NMR, including quantification of dynamics and /or structure determination. The candidate must have a Ph. D.

Contact information:
Dr. Magnus Wolf-Watz
Department of Chemistry
University of Umeå
Sweden
Email: magnus.wolf-watz@chem.umu.se
Phone: +46-90-786 76 90
Lab website: www.chemistry.umu.se

References:
1. Åden J., & Wolf-Watz M. (2007), JACS, 14, 14003-14012.
2. Wolf-Watz M., et al. (2004), Nat. Struct. Mol. Biol. ,11, 945-949.
3. Henzler-Wildman K., et al. (2007), Nature, 2007, 450, 838.
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