The solid-state NMR group at the University of Warwick would like to advertise the following University of Warwick scheme to fund post-doctoral research fellowships.
Candidates with strong CVs and publication records meeting the eligibility requirements (have passed PhD viva and be within 3 years of PhD graduation) are requested to contact
Steven Brown (S.P.Brown@warwick.ac.uk)
or John Hanna (J.V.Hanna@warwick.ac.uk)
by 15th February.
http://www2.warwick.ac.uk/fac/cross_fac/ias/prf/
Institute of Advanced Study
University of Warwick
Postdoctoral Research Fellowships (5 posts)
(£27,428 pa)
Fixed Term Contract for 2 years, beginning October 2011
The Institute of Advanced Study (IAS) at the University of Warwick invites applications from outstanding researchers who are at the beginning of a promising academic career. Applications are welcome from across all Faculties and disciplines, and, in keeping with the ethos of Warwick’s IAS, interdisciplinary research applications are strongly encouraged.
You will be based in the IAS but will have a strong presence in a home academic department. Therefore, all applications MUST be supported by a Warwick academic nominator and your proposed research project should closely complement your nominated academic department’s current research interests. Nominators will be required to make a strong case for the applicant’s strategic contribution to the research within their department.
You will have been awarded your PhD, or equivalent, in any discipline and be within 3 years of your PhD graduation. Therefore you must have passed your viva and submitted the final copy of your thesis to be eligible. You should also not have more than 3 years postdoctoral research/teaching experience or hold, nor have held, a permanent academic post.
Please note that although the Fellowships will be located in the IAS, you must be nominated by an academic in a Warwick department. The nomination form can be downloaded www.go.warwick.ac.uk/ias/prf .
Closing date: 8 March 2011
Steven Brown
Department of Physics
University of Warwick
Coventry CV4 7AL
Tel: 00 44 24 76574359
Fax: 00 44 24 76150897
email: S.P.Brown@warwick.ac.uk
webpage address: http://go.warwick.ac.uk/nmr/members/academic/steven/
Warwick group webpage: http://go.warwick.ac.uk/nmr/
The UK 850 MHz solid-state NMR facility: http://go.warwick.ac.uk/850mhz/
Magnetic Resonance at Warwick: Watch the video: http://go.warwick.ac.uk/nmr/millburn
getting to Millburn House: http://go.warwick.ac.uk/nmr/getting_here
Dienstag, 8. Februar 2011
Full Time Position
The Rock and Fluid Science Department of Shell Innovation, Research & Technology seeks a PhD graduate in Physics or equivalent sciences for a full-time position to further advance Magnetic Resonance Relaxometry and Magnetic Resonance Imaging technologies at its research facility in Houston, TX USA. The position will suit an experimental researcher with a background in MRI and NMR physics or engineering, who is interested in working in a more applied environment.
Further information related to this position, as well as a link to submit applications, can be found at:
http://impact-gs.jobstreet.com/templates/shell_my/jobdesc_global.aspx?eid=NKnk6pi3lDhEDJ%2b5ntow7TQhp7M%3d&uid=469%7c23089%7c%7c&did=0&its=0&src=8&ref=&cc=&agn=
The deadline for submitting applications is 28 February 2011.
Matthias Appel
Project Leader, Rock and Fluid Science Department
Shell Innovation, Research and Technology
Houston, TX, USA
Further information related to this position, as well as a link to submit applications, can be found at:
http://impact-gs.jobstreet.com/templates/shell_my/jobdesc_global.aspx?eid=NKnk6pi3lDhEDJ%2b5ntow7TQhp7M%3d&uid=469%7c23089%7c%7c&did=0&its=0&src=8&ref=&cc=&agn=
The deadline for submitting applications is 28 February 2011.
Matthias Appel
Project Leader, Rock and Fluid Science Department
Shell Innovation, Research and Technology
Houston, TX, USA
Postdoc Oxford
UNIVERSITY OF OXFORD
Department of Chemistry
Physical and Theoretical Chemistry Laboratory
Postdoctoral Research Assistant - NMR of photoactive proteins
Grade 07S : Salary £28,983 - £35,646 p.a.
Post Ref. DN11001/PJH
Applications are invited for a postdoctoral research assistant to work with Professor Peter Hore on a research project funded by DARPA (http://www.darpa.mil/). The post is available initially for up to 18 months, with a possible total duration of up to three years.
This position is part of a large project entitled Quantum Effects in Magnetoreception funded by the Defense Advanced Research Projects Agency as part of the programme Quantum Effects in Biological Environments (QuBE). The broad aims of the project are: (a) to design and perform a set of experiments that will determine definitively whether manifestly quantum effects are exploited in the avian magnetic compass sensor; (b) to develop the existing quantum mechanical model of magnetic effects on radical pair reactions; (c) to design and construct a proof-of-principle magnetic sensor around the reactions of radical pairs in model compounds. A central part of the project will involve optical and magnetic resonance experiments on the photo-active proteins photolyase and cryptochrome to establish their suitability as chemical sensors of weak magnetic fields.
The applicant should ideally have experience of protein NMR spectroscopy. The successful candidate will have the opportunity to work with colleagues from a range of disciplines on projects at the chemical/physical/life sciences interface.
The Hore group is located in the Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford, OX1 3QZ (www.chem.ox.ac.uk). To find out more about the group’s research, please visit http://research.chem.ox.ac.uk/peter-hore.aspx.
Applicants should either already have a PhD in a relevant subject area, or have submitted their thesis prior to taking up the post.
For further particulars of the post, including how to apply, please visit our website http://www.chem.ox.ac.uk/jobs.asp. These should be downloaded before an application is made. Informal enquiries should be addressed to peter.hore@chem.ox.ac.uk who would be pleased to supply further information about the project. Please quote reference DN11001/PJH in all correspondence.
The closing date for applications is 28 February 2011.
-----------------------------------------------------------------------
P J Hore
Department of Chemistry, University of Oxford
Physical and Theoretical Chemistry Laboratory
South Parks Road, Oxford OX1 3QZ, UK
Tel: +44 (0)1865 275415 Fax: +44 (0)1865 275410
Email: peter.hore@chem.ox.ac.uk
Website: http://hore.chem.ox.ac.uk/
-----------------------------------------------------------------------
Department of Chemistry
Physical and Theoretical Chemistry Laboratory
Postdoctoral Research Assistant - NMR of photoactive proteins
Grade 07S : Salary £28,983 - £35,646 p.a.
Post Ref. DN11001/PJH
Applications are invited for a postdoctoral research assistant to work with Professor Peter Hore on a research project funded by DARPA (http://www.darpa.mil/). The post is available initially for up to 18 months, with a possible total duration of up to three years.
This position is part of a large project entitled Quantum Effects in Magnetoreception funded by the Defense Advanced Research Projects Agency as part of the programme Quantum Effects in Biological Environments (QuBE). The broad aims of the project are: (a) to design and perform a set of experiments that will determine definitively whether manifestly quantum effects are exploited in the avian magnetic compass sensor; (b) to develop the existing quantum mechanical model of magnetic effects on radical pair reactions; (c) to design and construct a proof-of-principle magnetic sensor around the reactions of radical pairs in model compounds. A central part of the project will involve optical and magnetic resonance experiments on the photo-active proteins photolyase and cryptochrome to establish their suitability as chemical sensors of weak magnetic fields.
The applicant should ideally have experience of protein NMR spectroscopy. The successful candidate will have the opportunity to work with colleagues from a range of disciplines on projects at the chemical/physical/life sciences interface.
The Hore group is located in the Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford, OX1 3QZ (www.chem.ox.ac.uk). To find out more about the group’s research, please visit http://research.chem.ox.ac.uk/peter-hore.aspx.
Applicants should either already have a PhD in a relevant subject area, or have submitted their thesis prior to taking up the post.
For further particulars of the post, including how to apply, please visit our website http://www.chem.ox.ac.uk/jobs.asp. These should be downloaded before an application is made. Informal enquiries should be addressed to peter.hore@chem.ox.ac.uk who would be pleased to supply further information about the project. Please quote reference DN11001/PJH in all correspondence.
The closing date for applications is 28 February 2011.
-----------------------------------------------------------------------
P J Hore
Department of Chemistry, University of Oxford
Physical and Theoretical Chemistry Laboratory
South Parks Road, Oxford OX1 3QZ, UK
Tel: +44 (0)1865 275415 Fax: +44 (0)1865 275410
Email: peter.hore@chem.ox.ac.uk
Website: http://hore.chem.ox.ac.uk/
-----------------------------------------------------------------------
Mittwoch, 26. Januar 2011
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.
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.
Dear Colleagues,
I anticipate one or more openings for postdoctoral associates to work on structural and functional characterization of either proteins involved in vesicle trafficking or proteins involved in glycan interactions. These are challenging projects involving both protein-protein and protein-membrane associations. The work is well illustrated by our recent publication in Nature Structural and Molecular Biology (17(7):876-81, 2010). It is especially important that candidates have experience with advanced NMR methodology (either solution or solids) and are interested in the development of novel approaches to solving challenging problems in the structural biology area.
Our lab has access to excellent NMR instrumentation, including 800 and 900 MHz instruments with cryogenic probes. We also have strong biochemical collaborations that facilitate preparation and characterization of samples. Athens is a University town in the Southeastern part of the United States with excellent cultural amenities and a moderate cost of living. The position could begin as early as March 1, 2011, and we anticipate stable funding for several years.
Please forward this description to individuals who may be interested in the position and ask them to send a letter describing their interests, along with a CV and the names of three individuals we might contact for reference letters. The University of Georgia is an AA/EEO employer.
Sincerely, J.H. Prestegard
James H. Prestegard
Complex Carbohydrate Research Center
University of Georgia
315 Riverbend Rd
Athens, GA 30602-4712 USA
706-542-6281
jpresteg@ccrc.uga.edu
I anticipate one or more openings for postdoctoral associates to work on structural and functional characterization of either proteins involved in vesicle trafficking or proteins involved in glycan interactions. These are challenging projects involving both protein-protein and protein-membrane associations. The work is well illustrated by our recent publication in Nature Structural and Molecular Biology (17(7):876-81, 2010). It is especially important that candidates have experience with advanced NMR methodology (either solution or solids) and are interested in the development of novel approaches to solving challenging problems in the structural biology area.
Our lab has access to excellent NMR instrumentation, including 800 and 900 MHz instruments with cryogenic probes. We also have strong biochemical collaborations that facilitate preparation and characterization of samples. Athens is a University town in the Southeastern part of the United States with excellent cultural amenities and a moderate cost of living. The position could begin as early as March 1, 2011, and we anticipate stable funding for several years.
Please forward this description to individuals who may be interested in the position and ask them to send a letter describing their interests, along with a CV and the names of three individuals we might contact for reference letters. The University of Georgia is an AA/EEO employer.
Sincerely, J.H. Prestegard
James H. Prestegard
Complex Carbohydrate Research Center
University of Georgia
315 Riverbend Rd
Athens, GA 30602-4712 USA
706-542-6281
jpresteg@ccrc.uga.edu
Postdoc
Umeå University - with its 33,500 students and over 4,200 employees - is an organisation in constant change and development. Umeå University conducts groundbreaking research within several areas - several in which we are among the best in the world - within others regarded as the leaders in Sweden. We are one of Sweden’s largest providers of education and offer a broad and attractive range of courses and programmes. Our campus constitutes an inspiring environment for everyone that studies and works here. We wish to co-operate with companies and organisations throughout the Umeå region and all over the world.
2 postdoctoral positions (2 years)
in Protein Biophysics with focus on NMR applications and Copper transport
The research activities at the Department of Chemistry have a focus on Biological Chemistry, Biogeochemistry, and Technical Chemistry. Within the area of Biological Chemistry, one of the major directions is the study of protein folding, structure, and dynamics. Within the research group of Wittung-Stafshede, folding of metalloproteins and oligomeric proteins has been studied for many years by using strategic protein systems in combination with a range of biophysical/spectroscopic methods. The current major focus is on (a) understanding mechanisms of proteins involved in copper transport in the cytoplasm as well as on (b) effects of macromolecular crowding on protein biophysics. One postdoctoral fellow will study key proteins involved in copper transport (position 1), the other postdoctoral fellow will use NMR as a major tool to study proteins, for example in cell-like environments (position 2). Both projects are open to flexibility, new ideas and collaborations.
The candidates should have a Ph.D. in chemistry/biophysics/biology, or equivalent, which is not more than three years old. The person must have hands on experience with copper transport proteins (position 1) and training in solution NMR (position 2). For both positions, skills in protein expression and purification as well as basic protein thermodynamic/kinetic data analysis are necessary. Good communication skills in written and spoken English are required.
The application should include (1) a Curriculum Vitae, (2) copies of degree certificates and publications, (3) names and contact information to at least three reference persons and (4) a cover letter with a motivation.
The application can be submitted either electronically (MS Word or PDF format) or in hard-copy (two copies) form.
For further information about the positions, please contact Prof. Pernilla Wittung-Stafshede, phone: +46-(0)90 786 53 47, e-mail: pernilla.wittung@chem.umu.se.
Note: If you apply for both positions, two separate applications must be submitted.
Union information is available from SACO, +46-(0)90-786 53 65, SEKO, +46-(0)90-786 52 96 and ST, +46-(0)90-786 54 31.
Your complete application, marked with reference number 315-37-11 (position 1) or 315-38-11 (position 2), should be sent to jobb@umu.se (with reference number on the subject line) or in paper form to the Registrar, Umeå University, SE-901 87 Umeå, Sweden to arrive April 11, 2011 at the latest.
We look forward to receiving your application!
http://www8.umu.se/umu/aktuellt/arkiv/lediga_tjanster/315-37-11_315-38-11_sv_eng.html
contact:
Pernilla Wittung-Stafshede
Professor, Chemistry Department
Umeå University
901 87 Umeå, Sweden
pernilla.wittung@chem.umu.se
phone: 090-786 5347
2 postdoctoral positions (2 years)
in Protein Biophysics with focus on NMR applications and Copper transport
The research activities at the Department of Chemistry have a focus on Biological Chemistry, Biogeochemistry, and Technical Chemistry. Within the area of Biological Chemistry, one of the major directions is the study of protein folding, structure, and dynamics. Within the research group of Wittung-Stafshede, folding of metalloproteins and oligomeric proteins has been studied for many years by using strategic protein systems in combination with a range of biophysical/spectroscopic methods. The current major focus is on (a) understanding mechanisms of proteins involved in copper transport in the cytoplasm as well as on (b) effects of macromolecular crowding on protein biophysics. One postdoctoral fellow will study key proteins involved in copper transport (position 1), the other postdoctoral fellow will use NMR as a major tool to study proteins, for example in cell-like environments (position 2). Both projects are open to flexibility, new ideas and collaborations.
The candidates should have a Ph.D. in chemistry/biophysics/biology, or equivalent, which is not more than three years old. The person must have hands on experience with copper transport proteins (position 1) and training in solution NMR (position 2). For both positions, skills in protein expression and purification as well as basic protein thermodynamic/kinetic data analysis are necessary. Good communication skills in written and spoken English are required.
The application should include (1) a Curriculum Vitae, (2) copies of degree certificates and publications, (3) names and contact information to at least three reference persons and (4) a cover letter with a motivation.
The application can be submitted either electronically (MS Word or PDF format) or in hard-copy (two copies) form.
For further information about the positions, please contact Prof. Pernilla Wittung-Stafshede, phone: +46-(0)90 786 53 47, e-mail: pernilla.wittung@chem.umu.se
Note: If you apply for both positions, two separate applications must be submitted.
Union information is available from SACO, +46-(0)90-786 53 65, SEKO, +46-(0)90-786 52 96 and ST, +46-(0)90-786 54 31.
Your complete application, marked with reference number 315-37-11 (position 1) or 315-38-11 (position 2), should be sent to jobb@umu.se
We look forward to receiving your application!
http://www8.umu.se/umu/aktuellt/arkiv/lediga_tjanster/315-37-11_315-38-11_sv_eng.html
contact:
Pernilla Wittung-Stafshede
Professor, Chemistry Department
Umeå University
901 87 Umeå, Sweden
pernilla.wittung@chem.umu.se
phone: 090-786 5347
PhD Positions
4 PhD Positions in "Hyperpolarised 13C MR Imaging Methods"
Description:
The Technische Universität München (TUM) is seeking applications from highly motivated candidates for PhD (Dr. rer. nat.) positions in hyperpolarised magnetic resonance (MR) imaging. Hyperpolarised 13C metabolic imaging is a novel technique to investigate cellular processes and physiological parameters minimally invasive. You will be involved in developing and investigating MR methods for hyperpolarised imaging of novel biological contrast mechanisms. The four different positions focus on the following aspects of hyperpolarisation: alternative 13C-labelled agents, advanced MR methods for an efficient signal acquisition and reconstruction. Overall goal is to advance the diagnostic information of MR for applications including oncology and cardiology. Depending on the specific task this will require good physical, biological and chemical understanding. Candidates having previous experience in magnetic resonance will be preferred.
You will be collaborating with a team of experienced scientists from the MR group at GE, the Medical Engineering (Prof Haase), Chemistry (Prof Glaser) and Nuclear Medicine (Prof Schwaiger) departments at TUM, get unique access to latest hardware, as well as an extensive internal and external network of collaborating sites. The TUM and GE Global Research provide excellent infrastructure for conducting cutting-edge research.
Qualifications:
The applicant should have a Masters degree and a strong background in physics, electrical engineering, biochemistry, biology, chemistry or related subjects. Fluency in English is required.
Our offer:
The Ph.D. students will be employed by the TUM (3/4 TVöD E13; equivalent to other TUM PhD positions) and additionally members of the TUM graduate school which offers additional education in sciences and transferable skills courses and seminars.
Application Details:
Applications should include curriculum vita, certificates and transcript of BA/MA/Diplom or equivalent degree, summary of the previous work, letter of motivation and names of 2 references. Please send your application within one pdf-document to axel.haase@tum.de
Contact:
Prof. Axel Haase
TU München
IMETUM
Boltzmannstr. 11
85748 Garching
axel.haase@tum.de
http://www.imetum.tum.edu/
Description:
The Technische Universität München (TUM) is seeking applications from highly motivated candidates for PhD (Dr. rer. nat.) positions in hyperpolarised magnetic resonance (MR) imaging. Hyperpolarised 13C metabolic imaging is a novel technique to investigate cellular processes and physiological parameters minimally invasive. You will be involved in developing and investigating MR methods for hyperpolarised imaging of novel biological contrast mechanisms. The four different positions focus on the following aspects of hyperpolarisation: alternative 13C-labelled agents, advanced MR methods for an efficient signal acquisition and reconstruction. Overall goal is to advance the diagnostic information of MR for applications including oncology and cardiology. Depending on the specific task this will require good physical, biological and chemical understanding. Candidates having previous experience in magnetic resonance will be preferred.
You will be collaborating with a team of experienced scientists from the MR group at GE, the Medical Engineering (Prof Haase), Chemistry (Prof Glaser) and Nuclear Medicine (Prof Schwaiger) departments at TUM, get unique access to latest hardware, as well as an extensive internal and external network of collaborating sites. The TUM and GE Global Research provide excellent infrastructure for conducting cutting-edge research.
Qualifications:
The applicant should have a Masters degree and a strong background in physics, electrical engineering, biochemistry, biology, chemistry or related subjects. Fluency in English is required.
Our offer:
The Ph.D. students will be employed by the TUM (3/4 TVöD E13; equivalent to other TUM PhD positions) and additionally members of the TUM graduate school which offers additional education in sciences and transferable skills courses and seminars.
Application Details:
Applications should include curriculum vita, certificates and transcript of BA/MA/Diplom or equivalent degree, summary of the previous work, letter of motivation and names of 2 references. Please send your application within one pdf-document to axel.haase@tum.de
Contact:
Prof. Axel Haase
TU München
IMETUM
Boltzmannstr. 11
85748 Garching
axel.haase@tum.de
http://www.imetum.tum.edu/
Facility Manager/Research Scientist
The Singapore Bioimaging Consortium (SBIC) is one of the research institutes
under the Agency for Science, Technology and Research (A*STAR). SBIC aims to
advance imaging technology for understanding disease processes, early
diagnosis, and better prognosis in pre-clinical models, and their translation
into the clinic. There are several active research teams developing NMR and MRI
methods and analyses in collaboration with other groups using positron emission
tomography (PET), and optical techniques, with shared facilities in SBIC. There
are extensive collaborations with academic institutions and industry.
Facilities and Equipment:
The SBIC is located in the Helios building on the Biopolis campus. The NMR/MRI
facility currently hosts a state-of-the-art Varian 9.4 T and a Bruker 7 T
ClinScan MRI, a Bruker 400 MHz NMR spectrometer, a HyperSense dynamic
polarization system, a BioScan NanoSPECT/CT, and a Siemens microPET/CT.
A Facility Manager/Research Scientist position, for Nuclear Magnetic Resonance
(NMR) spectroscopy and Magnetic Resonance Imaging (MRI), is available at the
Singapore Bioimaging Consortium (SBIC). The successful applicant will be
responsible for managing, specifying new equipment, training users, and
maintaining the NMR/MRI facility to ensure scientific outcomes of the highest
standard.
Highly motivated candidates with prior experience in maintaining MRI/S systems
and with NMR spectroscopy will be preferred. Candidates with trouble-shooting
skills including that with RF coils, and performing quality control testing
will be preferred. Job responsibilities will include cryogen filling of the
magnets, software upgrades, instruction of users, and trouble shooting.
Experience with mapping B1/B0 homogeneity, calibrating RF pulses, and
fabrication skills for minor equipment such as animal holders for MRI-PET will
be an advantage.
The preferred background will include, but not be limited to biophysics,
biochemistry, chemistry, and physics. Experience with electronics, computer
systems administration (Linux/Unix and Windows), and programming languages are
desirable. The possibility will exist to run your own experiments and/or to
collaborate with others. Good organization and communication skills are
required to work with the multi-disciplinary teams.
For further information about SBIC staff, projects, and instrumentation, visit
our website: http://www.sbic.a-star.edu.sg/.
Or contact Philip Kuchel (on philip_kuchel@sbic.a-star.edu.sg) ...he has
recently taken over from Prof Sir George Radda as ED of the SBIC
Interested candidates should submit his/her resume to the following email
address: recruit@sbic.a-star.edu.sg.
under the Agency for Science, Technology and Research (A*STAR). SBIC aims to
advance imaging technology for understanding disease processes, early
diagnosis, and better prognosis in pre-clinical models, and their translation
into the clinic. There are several active research teams developing NMR and MRI
methods and analyses in collaboration with other groups using positron emission
tomography (PET), and optical techniques, with shared facilities in SBIC. There
are extensive collaborations with academic institutions and industry.
Facilities and Equipment:
The SBIC is located in the Helios building on the Biopolis campus. The NMR/MRI
facility currently hosts a state-of-the-art Varian 9.4 T and a Bruker 7 T
ClinScan MRI, a Bruker 400 MHz NMR spectrometer, a HyperSense dynamic
polarization system, a BioScan NanoSPECT/CT, and a Siemens microPET/CT.
A Facility Manager/Research Scientist position, for Nuclear Magnetic Resonance
(NMR) spectroscopy and Magnetic Resonance Imaging (MRI), is available at the
Singapore Bioimaging Consortium (SBIC). The successful applicant will be
responsible for managing, specifying new equipment, training users, and
maintaining the NMR/MRI facility to ensure scientific outcomes of the highest
standard.
Highly motivated candidates with prior experience in maintaining MRI/S systems
and with NMR spectroscopy will be preferred. Candidates with trouble-shooting
skills including that with RF coils, and performing quality control testing
will be preferred. Job responsibilities will include cryogen filling of the
magnets, software upgrades, instruction of users, and trouble shooting.
Experience with mapping B1/B0 homogeneity, calibrating RF pulses, and
fabrication skills for minor equipment such as animal holders for MRI-PET will
be an advantage.
The preferred background will include, but not be limited to biophysics,
biochemistry, chemistry, and physics. Experience with electronics, computer
systems administration (Linux/Unix and Windows), and programming languages are
desirable. The possibility will exist to run your own experiments and/or to
collaborate with others. Good organization and communication skills are
required to work with the multi-disciplinary teams.
For further information about SBIC staff, projects, and instrumentation, visit
our website: http://www.sbic.a-star.edu.sg/.
Or contact Philip Kuchel (on philip_kuchel@sbic.a-star.edu.sg) ...he has
recently taken over from Prof Sir George Radda as ED of the SBIC
Interested candidates should submit his/her resume to the following email
address: recruit@sbic.a-star.edu.sg.
Montag, 17. Januar 2011
Postdoc NMR / X-Ray Proteins
TWO Postdoctoral Positions in Structural determination of protein complexes using solution NMR and X-Ray Crystallography at the IRB Barcelona (SPAIN)
The protein NMR group of Dr. Maria J. Macias has openings for two postdoctoral positions to conduct solution NMR and X-Ray studies of proteins in complex with protein fragments and/or with RNA. No experience with protein expression and purification is required. Applicants should send by email to maria.macias@irbbarcelona.org the C. vitae including the list of their publications, a covering letter explaining the candidate interest in the positions and email addresses of two referees. Applications close on 15 February 2011.
Funding for the positions is provided for 1 year in the first instance, but applicants should be ready to apply for competitive fellowships. The IRB Barcelona International Postdoctoral Programme (Info at http://postdoc.irbbarcelona.org) is currently open with the application deadline next 15th of February. The offered positions correspond to the projects named "Structural and functional studies on the cpeb family of RNA-binding family of proteins" and "Structural studies on human transcription factors".
The protein NMR group of Dr. Maria J. Macias has openings for two postdoctoral positions to conduct solution NMR and X-Ray studies of proteins in complex with protein fragments and/or with RNA. No experience with protein expression and purification is required. Applicants should send by email to maria.macias@irbbarcelona.org the C. vitae including the list of their publications, a covering letter explaining the candidate interest in the positions and email addresses of two referees. Applications close on 15 February 2011.
Funding for the positions is provided for 1 year in the first instance, but applicants should be ready to apply for competitive fellowships. The IRB Barcelona International Postdoctoral Programme (Info at http://postdoc.irbbarcelona.org) is currently open with the application deadline next 15th of February. The offered positions correspond to the projects named "Structural and functional studies on the cpeb family of RNA-binding family of proteins" and "Structural studies on human transcription factors".
Mittwoch, 12. Januar 2011
Postdoc Membrane Proteins
Structural studies of membrane proteins by NMR
A post-doctoral position is available to work on the structural studies of a variety of
membrane proteins (cytochrome P450, cytochrome b5, cytochrome-P450-reductase,
and a combination of these proteins to probe protein-protein interactions)
and amyloid proteins using NMR spectroscopy. We are presently utilizing a combination
of high-resolution solution NMR and solid-state (static and MAS) NMR techniques to
solve high-resolution structures and characterize the dynamics of membrane proteins
embedded in suitable model membranes including micelles, isotropic bicelles, bicelles,
and lipid bilayers. Excellent solution and solid-state NMR facilities (spectrometers ranging
from 400 MHz to 900 MHz), protein expression capabilities, and computational facilities
are available.
Interested applicants should have experience in any of the following areas:
structural biology of proteins by solution NMR, solid-state NMR methods development,
solution NMR methods development to study protein dynamics.
For more details about our research projects and recent publications, please visit our website:
www.umich.edu/~ramslab.
If you are interested in working on these exciting projects in collaboration with highly
enthusiastic and dynamic group of researchers, please send your CV by email to:
ramamoor@umich.edu.
Ayyalusamy Ramamoorthy
Professor of Biophysics and Chemistry
University of Michigan
Ann Arbor
MI 48109-1055
www.umich.edu/~ramslab
A post-doctoral position is available to work on the structural studies of a variety of
membrane proteins (cytochrome P450, cytochrome b5, cytochrome-P450-reductase,
and a combination of these proteins to probe protein-protein interactions)
and amyloid proteins using NMR spectroscopy. We are presently utilizing a combination
of high-resolution solution NMR and solid-state (static and MAS) NMR techniques to
solve high-resolution structures and characterize the dynamics of membrane proteins
embedded in suitable model membranes including micelles, isotropic bicelles, bicelles,
and lipid bilayers. Excellent solution and solid-state NMR facilities (spectrometers ranging
from 400 MHz to 900 MHz), protein expression capabilities, and computational facilities
are available.
Interested applicants should have experience in any of the following areas:
structural biology of proteins by solution NMR, solid-state NMR methods development,
solution NMR methods development to study protein dynamics.
For more details about our research projects and recent publications, please visit our website:
www.umich.edu/~ramslab.
If you are interested in working on these exciting projects in collaboration with highly
enthusiastic and dynamic group of researchers, please send your CV by email to:
ramamoor@umich.edu.
Ayyalusamy Ramamoorthy
Professor of Biophysics and Chemistry
University of Michigan
Ann Arbor
MI 48109-1055
www.umich.edu/~ramslab
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