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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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Unread 07-30-2010, 03:58 AM
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Join Date: Jul 2010
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Default Investigator II

Investigator II in the Structural Biology Platform (SBP) within the Center for Proteomic Chemistry (CPC) of Novartis Institutes for Biomedical Research (NIIBR) in Basel, Switzerland.

As a member of a multidisciplinary research team, you will apply NMR based techniques to study protein targets and antigen-antibody as well as protein-ligand interactions in order to facilitate the drug discovery process. Your work will include the purification of isotope labeled proteins. You will also be involved in evaluating potential new structural biology projects, coordinating the efforts of small teams towards providing structural and biophysical data to impact drug discovery projects, and representing the Structural Biology Platform in multidisciplinary/multinational project teams.

We are looking for a highly talented and motivated scientist with a PhD in biochemistry or related disciplines plus 1-3 years of postdoctoral experience in an academic or industrial setting. The ideal candidate will have extensive experience in a broad range of NMR techniques and in the area of protein purification. He/she will have a sound knowledge of biochemistry, analytics and a strong interest in the biology of human diseases. Experience in the use of additional biophysical methods to characterise protein-protein or protein-ligand interactions or crystallography would be advantageous. The candidate should be strongly committed and display a high level of creativity and passion for project work. He/she will be a member of a multi-disciplinary, multi-national team of drug discovery professionals. Excellent oral and written communication skills are required.

Please apply online: www.novartis.com/careers (JobID: 70618BR)
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