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NMR processing:
MDD
NMR assignment:
Backbone:
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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:
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 01-26-2011, 04:27 PM
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Default Post-Doctoral Research Associate

Post-Doctoral Research Associate

Post-Doctoral Research Associate: Druggability of Multi-Subunit Protein Interfaces
Department of Chemistry
Vacancy Reference No: MA07682 Salary: £27,319-£35,646

Limit of tenure applies*

A postdoctoral position is available in the research group of Dr Alessio Ciulli to study the druggability of protein-protein interfaces within a family of multi-subunit E3 Ubiquitin Ligases involved in protein degradation. Our goal is to understand the molecular basis underlying small molecule recognition of native interfaces of multi-protein complexes and to exploit the information gained for the fragment-based design of novel chemical probes of biological function. The project will use a combination of structural, biophysical, computational and biochemical techniques to study protein-ligand and protein-protein interactions. For more information, please check our group website (http://www-ciulli.ch.cam.ac.uk/).

The successful candidate will have the opportunity to join the Cambridge Molecular Therapeutics Programme (see http://www.cmtp.cam.ac.uk/cmtp.html), an interdisciplinary initiative based in Cambridge to explore new strategies for drug discovery against cancer and infectious diseases. We are equipped with state-of-the-art facilities to conduct cutting-edge research in all aspects of modern chemical biology, structural biology and biophysics.

Applicants should have (or be about to receive) a PhD in chemistry, biochemistry, structural biology, or a related area. Proven experience in NMR spectroscopy, X-ray crystallography or related techniques in chemical/structural biology and structure-based drug design is essential. Some experience in synthetic organic chemistry or cell biology is desirable but not necessary. The ability to work in a creative, interdisciplinary and dynamic research environment at the interface of chemistry and biology is paramount, and good written and oral communication skills are essential.

The post is available from March 2011. Applications should include a CV, publications list, a cover letter summarising research experience and interests, contact details for three professional referees, and a completed form CHRIS/6 Parts I and III (downloadable from http://www.admin.cam.ac.uk/offices/hr/forms/chris6/), and should be sent to Dr Alessio Ciulli, Department of Chemistry, Lensfield Road, Cambridge CB2 1EW (email: ac313@cam.ac.uk).

* The funds for this post are available until December 31st 2012 in the first instance.

Closing date: 28 February 2011.

The University values diversity and is committed to equality of opportunity.

The University of Cambridge only advertises their own and college vacancies on this website; we do not advertise any external vacancies.

The University has a responsibility to ensure that all employees are eligible to live and work in the UK.


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