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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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Thread Tools Search this Thread Rating: Thread Rating: 1 votes, 5.00 average. Display Modes
  #1  
Old 08-17-2010, 02:02 PM
Junior Member
 
Join Date: Aug 2010
Posts: 1
Points: 22, Level: 1
Points: 22, Level: 1 Points: 22, Level: 1 Points: 22, Level: 1
Level up: 43%, 28 Points needed
Level up: 43% Level up: 43% Level up: 43%
Activity: 33.3%
Activity: 33.3% Activity: 33.3% Activity: 33.3%
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NMR Points: 22
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Default Protein NMR/Biophysics Research Associate (BS/MS)

The candidate will join a state-of-the art protein structure unit at the Novartis Cambridge, MA USA campus as part of the protein NMR team. Core responsibilities will include sample preparation logistics and data collection to support both fragment based drug discovery and HTS hit validation. In addition, the candidate will participate in the maintenance and incorporation of new technologies to support these efforts. Opportunities for scientific growth in the interpretation and design of experiments will be available. The successful candidate will have demonstrated successes in working in a collaborative, multidisiplinary environment. Candidates with experience in protein chemistry, automation technologies, and/or Linux computer environments will be at a decided advantage.

Minimum requirements are a B.S/M.S. or equivalent in biochemistry or a related discipline with at least 2 years of research laboratory experience. Experience in protein handling/characterization and laboratory automation is required. Attention to detail, an ability to work independently, and multitasking skills are expected. Experience with NMR spectroscopy and/or biophysical characterization of proteins and computational skills would be a decided asset. The candidate must possess good oral and written communication skills and should be able to function well in a matrix managed environment.





Please apply online: www.novartis.com/careers (JobID: 70998BR)
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