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NMR processing:
MDD
NMR assignment:
Backbone:
Autoassign
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:
PROSESS
PSVS
RPF scores
iCing
Chemical shifts:
PROSESS
CheShift2
Vasco
iCing
RDCs:
DC
Anisofit
Pseudocontact shifts:
Anisofit
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:
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:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
UPLABEL
Solid-state NMR:
sedNMR


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Old 09-15-2010, 04:10 PM
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Default Postdoc Paris

Postdoc Paris

A two-year postdoctoral position is available in the NMR group headed by Prof. G. Bodenhausen in "Laboratoire des Biomolécules" in Paris (France), under the supervision of Prof. O. Lequin.

The selected candidate will be involved in a project which aims at analyzing structure-function relationships of homeoproteins. Homeoproteins form a large class of transcription factors characterized by a conserved DNA binding domain called homeodomain. These proteins possess the striking property to be internalized within cells by direct membrane translocation processes which are not yet well understood. Homeoproteins are thus involved in original modes of cell signalling. The work of the selected candidate will mainly focus on studying the structure and interactions of homeodomains in aqueous environments, in membrane environments and in cellular environments. This project is funded by the French Agence Nationale pour la Recherche (ANR grant "PARAHP") and will be carried out in collaboration with biochemists and cell biologists (groups of A. Joliot, A. Prochiantz, L. Venance, CNRS-INSERM-Collège de France).

The candidate should have a strong expertise in NMR spectroscopy and be motivated in developing multidisciplinary research fields including liquid state NMR, solid state NMR of protein/lipid complexes, in cell NMR, and biochemistry (protein expression, membrane models, cell culture).

Contact: olivier.lequin@upmc.fr
Laboratoire des Biomolécules, UMR 7203
Université Pierre et Marie Curie – ENS – CNRS


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