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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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Default Postoctoral position in Structural Biology

Postoctoral position in Structural Biology

UNIVERSITY OF OXFORD
DEPARTMENT OF BIOCHEMISTRY

Postdoctoral Research Associate in Structural Biology

We are seeking to appoint a highly motivated Postdoctoral Research
Associate in the laboratory of Dr. Ioannis Vakonakis for studies of
proteins involved in centriole assembly. The successful candidate will
join a multidisciplinary collaboration between Oxford and the groups of
Prof. Pierre Gönczy (EPFL) and Dr. Michel Steinmetz (Paul Scherrer
Institute) in Switzerland. Recently, our joint efforts elucidated the
origins of centriolar 9-fold symmetry (Kitagawa, Vakonakis et
al.,Cell144, 364-375, 2011), a critical step in the centrosomal
duplication process that ensures genome stability in animals. We now
seek to build upon this breakthrough by studying the structure/function
relationship of centriolar components such as SAS-6, SAS-5, SAS-4,
ZYG-1, SPD-2 and others. The successful candidate will contribute to the
analysis of these targets using structural (crystallography, solution
NMR and/or small angle scattering) and biophysical methods.


Applicants should possess/be expected to obtain a PhD in natural
sciences and should have experience in aspects of the structural biology
pipeline, for example protein production and purification, NMR
spectroscopy or X-ray crystallography. Past experience with
complementary biophysical techniques (ITC, AUC, CD etc) and biomolecular
interactions is desirable. Previous familiarity with centriolar or
relevant biological systems would be an advantage but is not essential.


This full-time post is funded by the Biotechnology and Biological
Sciences Research Council (BBSRC)for up to three years in the first
instance and is based in the New Biochemistry building, South Parks
Road, Oxford. More information about our group can be found by clicking
on the link below:


http://www2.bioch.ox.ac.uk/~rrnmr


This position is graded on the University’s grade 7 scale, for which the
salary range is £29,099 - £35,788 per annum. The actual starting salary
offered will be based on qualifications and relevant skills acquired and
will also be determined by the funding available.


For further general information, phone (01865) 613204, quoting reference
number BR/493.


Applications for this vacancy are to be made online.


To apply for this role and for further details, including the job
description and selection criteria,

please click on the link below:

https://www.recruit.ox.ac.uk/pls/hri...ec?p_id=101979

The closing date for applications is Monday, 20thFebruary 2012. It is
envisioned that interviews for shortlisted candidates will take place
within approximately 10-14 days.

The University of Oxford is committed to equality and values diversity


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