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NMR processing:
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Side-chains:
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UNIO Candid
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Ab initio:
GeNMR
Cyana
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UNIO ATNOS-Candid
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Fragment-based:
BMRB CS-Rosetta
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Template-based:
GeNMR
I-TASSER
Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
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Homology-based:
CS23D
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Torsion angles from chemical shifts:
Preditor
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Secondary structure from chemical shifts:
CSI (via RCI server)
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Flexibility from chemical shifts:
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Interactions from chemical shifts:
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Chemical shifts re-referencing:
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Molecular dynamics:
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From structure:
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From sequence:
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Camcoil
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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 12-01-2010, 08:36 PM
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Default PhD Studentship

PhD Studentship

PhD Studentship Advertisement

Hosting organizations: Institute of Food Research, University of East Anglia, and John Innes Centre

Title: Allergen thermodynamics: The effect of structure and dynamics on the susceptibility of pollen and food allergens to proteolysis
Start date: October 2011
Deadline for applications: 6 December 2010
Project details:
The goal of the project is to define how protein structure and dynamics determine the susceptibility of birch pollen allergen and its homologues to low pH proteolysis. This knowledge will provide the rational basis for development of in silico methods for predicting digestibility of proteins, a cornerstone of genetically modified organism (GMO) allergenicity risk assessment.
We propose to compare the pH-induced unfolding pathways of birch pollen allergen superfamily members (Bet v 1, Mal d 1 and Api g 1), define its impact on patterns and pathways of proteolysis, and investigate the effects of mutations on this process. Unfolding will be characterised using CD, FT-IR and NMR spectroscopy as a function of pH. Unfolding experiments will be also performed in silico using Molecular Dynamics simulations on Cray supercomputer. In silico denatured states will
be compared against NMR results, thus describing the contribution of entropic and enthalpic processes to unfolding.
The student will receive a broad training in protein structure and characterisation, spanning protein biochemistry, heterologous expression and purification, proteolysis, proteomics, low resolution spectroscopy (fluorescence, CD and FT-IR) together within silico protein structure modelling and IgE-binding studies. This will be complemented by training in protein NMR spectroscopy, covering
multidimensional spectral acquisition, processing and assignment, structure calculation, and relaxation analysis. In addition to experimental studies the student will be trained to undertake molecular dynamics techniques for protein unfoldingin silico. Transferable skills training will include
presenting to and interacting with Professor Mills Food and Health Network Allergy cluster which includes industry and academic researchers with an interest in allergy.
Qualifications:
The candidate should be able to demonstrate an aptitude for structural biology. The particular areas include protein biochemistry, protein NMR, and structural biology.
Funding:
The studentship covers UK/EU tuition fees and an enhanced rate stipend in the region of £16,600 per annum as a result of funding restrictions it is available only to UK/EU students. Overseas student should NOT apply. Successful applicants will be interviewed as part of the studentship competition.
Enquiries:
Informal enquiries regarding the project should be directed to the project supervisors:
Clare Mills E-mail: clare.mills@bbsrc.ac.uk
Tharin Blumenschein E-mail: t.blumenschein@uea.ac.uk
Web-pages:
http://www.ifr.ac.uk/profile/clare-mills.as
http://www.uea.ac.uk/che/tb
How to apply:
For further information and an application form, please visit the 'How to Apply' page on our
website:
http://www.ifr.ac.uk/students/admissions.htm
Contact information:
Graduate Studies Office, John Innes Centre, Norwich Research Park,
Colney, Norwich, NR4 7UH, UK
Telephone: +44(0) 1603 450768
E-mail:graduates.nrp@bbsrc.ac.uk
-----------------------------------------
Dr. Tharin Blumenschein, Lecturer
t.blumenschein@uea.ac.uk
School of Chemistry
University of East Anglia
Norwich - NR4 7TJ
United Kingdom
Phone: +44 (0)1603 59 2963


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