Mittwoch, 6. Juni 2007

Group leader, Postdoc and PhD position University of Regensburg

Group leader position, structural biology/bioinformatics, Regensburg

The department of Biophysics (chair: H. R. Kalbitzer) is focused on
problems of structural biology with the methodological focus on magnetic
resonance spectroscopy, especially high-pressure NMR spectroscopy,
in-vitro-translation and the development of programs for the automated
NMR structure determination
(http://www.biologie.uni-regensburg.de/Biophysik/
Kalbitzer/index.html). Biochemical topics are the intracellular signal
transduction, ionic channels, membrane transport systems, systems
biology, metabonomics, and rational drug design. In bioinformatics we
develop together with Bruker Biospin programs for the automated analysis
of NMR spectra and structure determination (AUREMOL).

Applicants should have a strong interest in biological, structure
related questions. Besides own projects they should work on the
development of the program AUREMOL together with diploma and doctoral
students and other postdocs. They should have a PhD and experience in
the field of biological NMR spectroscopy of proteins and program
development.

The salary is according to A13 (Akademischer Rat auf Zeit) that is
depending on age and marital status approximately 50,000 Euro/year.
Initially, the position is limited to 3 years. Candidates planning to do
a Habilitation are favoured.

The institute is equipped with a Bruker Avance-500, a Bruker
Avance-600, and a Bruker Avance 800 spectrometer with cryoprobes. It has
access to the 900 MHz spectrometer in Munich.

Applications including a curriculum vitae, a list of publications and
the names of two referees should be sent by June 15, 2007 to

Prof. Dr. Dr. H. R. Kalbitzer
Institut fuer Biophysik und
Physikalische Biochemie
Universitaet Regensburg

D - 93040 Regensburg

Email hans-robert.kalbitzer@biologie.uni-regensburg.de

Postdoc position and PhD position

Postdoc and PhD-position in NMR based structural biology
at the
Institute of Biophysics and Physical Biochemistry, University of
Regensburg

Topic: Structure and function of the interaction domain of a
Ca2+-channel.
The department of Biophysics (chair: H. R. Kalbitzer) is focused on
problems of structural biology with the methodological focus on magnetic
resonance spectroscopy, especially high-pressure NMR spectroscopy,
in-vitro-translation and the development of programs for the automated
NMR structure determination
(http://www.biologie.uni-regensburg.de/Biophysik/
Kalbitzer/index.html). Biochemical topics are the intracellular signal
transduction, ionic channels, membrane transport systems, systems
biology, metabonomics, and rational drug design. In bioinformatics we
develop together with Bruker Biospin programs for the automated analysis
of NMR spectra and structure determination (AUREMOL).

Applicants should have a strong interest in biological, structure
related questions. The postdoc should have experience in the field of
biological NMR spectroscopy of proteins, the PhD-student in protein
biochemistry or crystallography.

The salary of the postdoc is according to TVL13 that is depending on
age and marital status approximately 50,000 Euro/year. Initially, the
position is limited to 2.5 years but can be prolonged further. The
salary of the PhD-student would correspond to TVL13/2 (approximately
25,000 Euro).

The institute is equipped with a Bruker Avance-500, a Bruker
Avance-600, and a Bruker Avance 800 spectrometer with cryoprobes. It has
access to the 900 MHz spectrometer in Munich.
In the project the structure of the cytoplasmic interaction domain
should be solved by NMR-spectroscopy and/or X-ray crystallography. Six
different interaction partners are available as recombinat proteins in
Regensburg and will be used for interaction studies. The Postdoc should
mainly concentrate on NMR spectroscopy, the PhD-student (cooperating
with the postdoc) should be responsible for protein expression,
crystallisation and functional applications of NMR spectroscopy.
Applications including a curriculum vitae, a list of publications and
the names of two referees should be sent by June 15, 2007 to

Prof. Dr. Dr. H. R. Kalbitzer
Institut fuer Biophysik und
Physikalische Biochemie
Universitaet Regensburg

D - 93040 Regensburg

Email hans-robert.kalbitzer@biologie.uni-regensburg.de

PhD Liquid State NMR

PhD Liquid State NMR

A PhD position in Liquid states NMR is open at the university of Geneva.
More info at

http://www.unige.ch/sciences/chiorg/jeannerat/

Dr. Damien Jeannerat,

PhD Southampton

PhD Southampton

Research Fellow: Molecular Interactions in Biological Membranes
£24,402 to £30,013 (starting salary £24,402)

School of Biological Sciences, University of Southampton

This post is funded by the Wellcome Trust to study molecular interactions in
biological membranes using solid-state NMR. The project focuses on studying
the interaction between the lipid bilayer and integral membrane proteins to
understand how they modulate protein function and regulate intracellular
protein trafficking, a process which has been linked to the onset of a range
of diseases including muscular dystrophy. The research exploits a variety of
biophysical and biochemical techniques to support solid-state NMR studies
characterizing the structure and dynamics of integral membrane proteins
within the lipid bilayer.

You will be an enthusiastic graduate with a recent PhD in Biochemistry, or a
related field with experience in membrane protein expression and purification
and an interest/background in using biophysical techniques including NMR
spectroscopy to understand how biological membranes function at a molecular
level.

The School of Biological Sciences has a highly active and interdisciplinary
research program with excellent experimental and computational facilities for
structural biology. This post is available for three years from 1 September
2007, or an earlier start date can be negotiated.

For further details you are welcome to contact Philip Williamson, tel.
023 8059 4350, email P.T.Williamson@soton.ac.uk, www.sbs.soton.ac.uk/staff/

To apply on-line, please click on the link below. Alternatively
telephone 023 8059 2750. The closing date for this post is 29th June
2007 at 12 p.m. Please quote reference number 1112-07-M on all
correspondence.

Solid State NMR Position

Solid State NMR Position

Project: Structural Investigations of b-sheet polymer hybrids using advanced solid-state NMR techniques.

Job description
Within the Physical Chemistry / solid-state NMR group of the Institute for Molecules and Materials, there is an opening for a graduate student for the study of biomimetic materials using advanced solid-state NMR techniques. The project will be dedicated to detailed structural investigations of b-sheet polymer hybrids developed in the synthetic groups in the IMM.

Requirements
Required education/skills:
We are looking for an enthusiastic researcher with a Master’s degree in Chemistry with adequate theoretical and experimental skills. We prefer candidates with a good team spirit, who like to work in an internationally oriented environment and are able to collaborate with our partner groups on the crossroads between chemistry and physics.

Conditions of employment
Estimated maximum salary per month: € 2000 - 2500

* Employment basis: Temporary for specified period
* Duration of the contract: Starts for a period of one year, with a possible prolongation till 4 years
* Maximum hours per week: 40

Further Information / application
Further information can be obtained from Prof. dr. A.P.M. Kentgens (e-mail a.kentgens@nmr.ru.nl, phone +31-24-3652078/3652004).
Written applications, including curriculum vitae, summary of research interest and experience, should be directed to: Mrs. A. Schröder, Faculty of Science, Personnel Department, Toernooiveld 1, 6525 ED Nijmegen, The Netherlands, or via e-mail pz@science.ru.nl

Project details
The aim of Institute for Molecules and Materials is to conduct research and train undergraduate and graduate students in the field of functional- molecular structures and materials. There is an emphasis on understanding and controlling complexity in order to be able to design new functionality in these systems. This research area can be divided into two main themes: bio-inspired systems and nano/mesoscopic structures. Covering both experimental and theoretical physics and chemistry, and harboring skills in state-of-the-art analytical and synthetic techniques, the groups that constitute the IMM possess expertise in all areas needed to explore these fields. Nuclear magnetic resonance (NMR) research plays an important role in the research of the IMM. The nuclear spin is a universal probe for local structural information which can contribute significantly to the level of understanding if applied under the proper conditions. The IMM has excellent solid-state NMR facilities, including Chemagnetics CMX Infinity 300, 400 and 600 MHz spectrometers, a homebuilt 180 MHz spectrometer and access to a Varian Inova 800 spectrometer with solids capabilities. In collaboration with the Nijmegen high magnet field laboratory 30 T Bitter magnet is being optimized for magnetic resonance experiments. Finally funds have been acquired to set up an international solid-state NMR facility including a new wide-bore 850 MHz NMR spectrometer that should arrive in 2008.
Materials scientists at IMM have become increasingly interested in combining natural and synthetic polymers into hybrid polymeric structures. The functionality of (fragments of) biopolymers can be integrated with the synthetic versatility and adaptability of synthetic polymers, thus creating a new class of materials harnessing the best of both worlds. One of the most common peptide motifs that have been introduced in polymer peptide hybrid materials is the b-sheet. Reasons for this are the synthetic accessibility of b-sheet forming peptides, small sequences already display the desired properties, and their relevance in structural proteins such as silk, in which (anti-parallel) b-sheets are responsible for crystallinity and hence stiffness of these biopolymers. More mobile regions are also present giving the material elasticity resulting in a material that is both very strong and smooth. The different physical properties of various silks arise from a variation in the protein’s primary and secondary structure.
IMM researchers (Prof. van Hest et al.) are working on controlled assembly of macromolecular -sheet fibrils. The attachment of poly(ethylene glycol) end blocks to a central poly(AG)3EG b-sheet block prevents the macroscopic aggregation of the b-sheet blocks into needle-shaped lamellar crystals. Instead crystallization results in well-defined fibrils. The rationale behind attachment of synthetic polymer blocks at the N- and C-termini was to restrict macroscopic crystallization and to preserve translation of the b-sheet design characteristics of width, height, and surface functionality into self-assembled structures. It is the subject of this study to develop and apply advanced solid-state NMR techniques to gain in-depth knowledge of the structure of these materials in relation to their functionality.
In some cases aggregation of b-sheet peptides is an undesired feature. This is particularly
true for fibril formation of b-amyloid peptide, the primary component of amyloid plaques in Alzheimer’s disease. One possibility is to prevent the aggregation of A by short peptide sequences. The goal is to study binding of the elongated peptides to the A monomers during the formation of oligomers and fibrils by solid-state NMR.

SPECTROSCOPIST

SPECTROSCOPIST (Nuclear Magnetic Resonance)

School of Chemical Sciences
University of Illinois at Urbana-Champaign


The School of Chemical Sciences at the University of Illinois at Urbana-Champaign is seeking applicants for Spectroscopist in its Nuclear Magnetic Resonance Laboratory. This facility primarily supports research in the Departments of Chemistry and of Chemical and Biomolecular Engineering. This full-time academic professional position requires a broad range of professional and technical skills. Minimum qualifications include a Ph.D. degree in Chemistry or related field, with specialization in NMR spectroscopy, or the equivalent experience in NMR spectroscopy.

The successful applicant will be a hands-on spectroscopist but also responsible for working with faculty, students, and staff. The skills sought include experience in configuring spectrometers and performing multidimensional biomolecular NMR experiments. Some experience is required in both multi-nuclear solution and solid state NMR, as well as computational skills for processing and analyzing 2D and 3D protein NMR data sets, assigning spectra, and computing protein structures from NMR restraint sets. At least some familiarity with the following software packages (or closely related alternatives) therefore is essential: Felix, NMRPipe, Sparky, NMRView, XPLOR, DYANA, MolMol, VMD. The laboratory contains the following instruments: Varian Unity 400, Varian Unity 500, Varian Unity Inova 300WB, Varian Unity Inova 500 (2), Varian Unity Inova 600, Varian Unity Inova 750 and Varian Infinity Plus 500WB. The Inova 750 and InfinityPlus 500WB are equipped for modern multidimensional magic-angle spinning experiments for proteins.

Salary: Commensurate with qualifications.

Starting date: As soon as possible after closing date of July 2, 2007.

Closing Date: For full consideration, all application materials (including cover letter, curriculum vitae, 3 letters of reference) must be received by the closing date of July 2, 2007. Applicants may be interviewed before the closing date; however, no hiring decision will be made until after that date.

Application: SCS prefers that applications be submitted online. To submit an application electronically, go to http://www.scs.uiuc.edu/scs_applicants and include a cover letter, curriculum vitae, and three references. We strongly recommend that you fill out the online application form as soon as you have assembled the names and email addresses of 3 references. This will create your application file, after which you (and your letter writers) will be able to upload application documents and reference letters. If necessary, applications could be mailed to: Attn: NMR Spectroscopist Search Committee, School of Chemical Sciences, 106 Noyes Lab, 505 S. Mathews Ave., Urbana, IL 61801. Minorities, women, and other designated class members are encouraged to apply.

The University of Illinois is an Affirmative Action/Equal Opportunity Employer.

Research Officer/Senior Research Officer

Research Officer/Senior Research Officer in Structural Genomics
Institute for Molecular Bioscience, Australia


More details below:

The research group led by Professor Glenn King at the Institute for Molecular
Bioscience (http://imb.uq.edu.au) is focused on drug and insecticide
discovery and the implementation of high-throughput techniques for protein
structure determination using NMR spectroscopy.

The Role: The successful candidate will be the lead structural biologist in a
novel and ambitious structural and functional genomics initiative that aims
to provide the first complete structure-function overview of the venom
proteome of a venomous animal. The majority of NMR experiments will be
performed using a state-of-the-art cryoprobe-equipped 900 MHz NMR
spectrometer.

The Person: Applicants should possess a PhD in structural biology,
biophysics, biochemistry, or protein chemistry and extensive practical
experience with elucidation of protein structures using 3D triple-resonance
NMR techniques.

Selection Criteria: The position description and selection criteria can be
obtained online (http://www.uq.edu.au/jobs/2005documents/imb/1124852.doc), or
by contacting Barb Clyde by phone (+61 7 3346 2121) or email
(b.clyde@imb.uq.edu.au).

Remuneration: This position is a full-time, fixed term appointment at
Research Academic Level A for 30 months initially, with ongoing renewal
subject to funding. Appointment at Academic Level B will be considered for
outstanding candidates with appropriate experience and skills. The
remuneration package will be in the range of AUS $54,289 to $73,639 per annum
(Academic Level A) or AUS $77,515 to $92,048 per annum (Academic Level B),
which includes employer superannuation contributions of 17% (equivalent to a
401K plan in the USA). The appointment will be at a level commensurate with
the successful candidate?s experience.

Contact: For further details, contact Professor Glenn King by phone (+61 7
3346 2025) or email (glenn.king@imb.uq.edu.au).

Submission of applications: Send applications, preferably by email
(b.clyde@imb.uq.edu.au), to the Human Resource Consultant, Institute for
Molecular Bioscience, The University of Queensland, St Lucia, QLD 4072,
Australia.

Closing Date for Applications: 1 July, 2007

Job Reference Number: 1124852

Postdoctoral research position

Postdoctoral research position in the Akke group at Biophysical Chemistry and the Center for Molecular Protein Science, Lund University

We are looking for highly motivated candidates to engage in challenging projects on biomolecular dynamics using NMR spectroscopy. We work in several areas, including protein folding, enzyme dynamics, and ribosome function.

The successful candidate has a strong background in NMR spectroscopy, and preferably in the development and application of multinuclear and multidimensional techniques towards biomolecular studies. Prior experience in protein expression and purification is a plus, but not a requirement.

The position is available from September 2007. Your application should include a statement of research interest, CV, and the names and e-mail addresses of 2-3 senior scientists (advisors etc) who are willing to provide letters of recommendation.

General information:
We have one 500 MHz and one 600 MHz Varian system of the latest generation (VnmrS), both equipped with 4 channels and pulsed field gradients. Access to higher fields (800 and 900 MHz Varian systems) and cryogenic probes are available off site at the Swedish NMR Center.
In addition, the department is equipped with a variety of biophysical instrumentation including CD, fluorescence, microcalorimetry, stopped-flow, surface plasmon resonance, light scattering, X-ray crystallography and mass spectrometry.
We are part of the Center for Molecular Protein Science, a dynamic and multidisciplinary research environment ( http://www.mps.lu.se/ ) that covers a wide range of research in molecular protein science.

More information about our research and recent publications can be found on our webpage:
http://www.bpc.lu.se/staff/groups/mikaels_group.html
http://www.bpc.lu.se/staff/personal/mikael_akke.html

For more information on the different project, please contact:
Mikael Akke, mailto:mikael.akke@bpc.lu.se