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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 03-14-2011, 05:44 PM
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Default postdoctoral position King's College

postdoctoral position King's College

A postdoctoral position supported by the King's College London British Heart Foundation Centre of Excellence is available at King's College London in the field of ROS biology. The project is a collaborative effort amongst the groups of Prof Ajay Shah MD (Cardiovascular Division, King's College London), Dr Conte and Dr Steiner (Randall Division of Cell and Molecular Biophysics, King's College London) aimed at elucidating the molecular mechanism of controlled ROS production in higher organisms.

The project is highly interdisciplinary and will combine structural biology (X-ray and NMR) with biophysical (ITC), biochemical and cell biology work. The post requires experience in molecular biology/protein biochemistry. Proven prior experience in protein expression using the baculovirus system is also considered very important. Additional experience with biophysical methods complementary to structural biology and/or oxygen biochemistry is welcomed.

The post is available immediately and funding is initially for 18 months. Salary will be commensurate to prior experience and qualifications. Interested applicants should contact Dr Maria R Conte (sasi.conte@kcl.ac.uk) directly by submitting their CV together with the names of three referees. Informal inquiries are welcome.

Deadline for this application is 21st March 2011.

---------------------------------------------------------------------
Maria R Conte
Reader in Structural Biology
Randall Division of Cell and Molecular Biophysics
King’s College London
New Hunt’s House
Guy’s Campus
London SE1 1UL, United Kingdom

Tel +44 (0)20 7848 6194
Fax +44 (0)20 7848 6435
Email sasi.conte@kcl.ac.uk
sasi.conte@hotmail.com[IMG]https...s.blogspot.com[/IMG]


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