2005 SGMS Meeting

The SGMS annual meeting was held on October 27 / 28, 2005, at the Mercure Hotel Beatenberg (formerly Hotel Dorint)... high above Lake Thun in the Bernese Oberland, with a scenic view of the Swiss Alps!

Programme

Thursday 2005-10-27
	Starting Session Chair: Andreas Stämpfli, Hoffmann-La-Roche, Basel
11:15 - 11:30	Welcome Note
11:30 - 12:15	Marcel Mayor Molecular Electronics: Devices of Tomorrow?
12:30 - 14:00	Lunch
	Session 1 Chair: Laurent Bigler, University of Zürich
14:00 - 14:45	Eric Forest, CEA Grenoble, France Use of Mass Spectrometry to Study the Structure and the Interactions of Proteins.
14:45 - 15:05	Kenneth Tomer, NIEHS/NIH, Research Triangle Park, NC, USA Mass Spectrometric Characterization of Infectious Disease Epitopes Recognized by Human Monoclonal Antibodies
15:05 - 15:25	Patrice Waridel, MPI, Dresden, Germany Homology-driven Proteomics in Organisms with Unsequenced Genome by Automated LC-MS/MS de Novo Sequencing and MS Blast Search
15:25 - 15:45	Arnd Ingendoh, Bruker Daltonik GmbH, Bremen, Germany Combining Novel Fragmentation and Front-end Enrichment Techniques for Highly Increased Sensitivity and Selectivity of Phosphopeptide Detection
15:45 - 16:15	Coffee Break
	Session 2 Chair: Jean-Luc Wolfender, University of Geneva
16:15 - 16:35	Richard Knochenmuss, Novartis, Basel, Switzerland Looking Deeper into MALDI: Understanding and Predicting MALDI Phenomena using Numerical Models
16:35 - 16:55	Victor J Nesatyy, Eawag, Dübendorf, Switzerland Investigating the Mechanism of Cd-binding by the Rainbow Trout Estrogen Receptor using ICP/MS and MALDI-TOF
16:55 - 17:15	Jan Tromp, University of Bern, Bern, Switzerland Gas Phase Dissociation of RNA
17:30	General Assembly 2005
19:00	Apéro
20:00	Blüemlisalp Dinner Buffet
Friday 2005-10-28
	Session 3 Chair: Stephan Brombacher, Novartis Pharma AG, Basel
08:30 - 09:15	Gary L. Glish, University of North Carolina, Chapel Hill, NC, USA The Quadrupole Ion Trap and Proteomics: New Developments in Top Down and Bottom Up Analysis
09:15 - 09:35	Fabian Kuhn, Givaudan Schweiz AG, Dübendorf, Switzerland Side Product Analysis of Minor Constituents in Perfumery Raw Materials Using Two-dimensional Gas Chromatography Coupled to Mass Spectrometry
09:35 - 09:55	Jana Hüttig, University of Basel, Basel, Switzerland Determination of Chloroparaffins in Sediments by High Resolution Gas Chromatography Coupled to Mass Spectrometry with Different Ionization Techniques
09:55 - 10:15	Ines Burkard, University Hospital Zurich, Zurich, Switzerland Bile Acid Pattern – Quantification of Uncomjugated, Glycine- and Taurine-conjugated Bile Acids
10:15 - 10:45	Coffee Break
	Session 4 Chair: Marc J-F Suter, Eawag, Dübendorf
10:45 - 11:30	Thorsten Reemtsma, TU Berlin, Berlin, Germany Insight into Fulvic Acid Molecules by Electrospray Mass Spectrometry
11:30 - 11:50	Ingrid Langlois, University of Basel, Basel, Switzerland Perfluorooctane Sulfonate Analysis and its close Relationship with Mass Spectrometry
11:50 - 12:10	Anton Kaufmann, Kantonales Labor, Zürich, Switzerland Sub-2 µm Particulate HPLC Columns for LC-MS-(MS): Benefits and Limitations
12:10 - 12:30	Winfried Wagner-Redeker, Spektronex AG, Basel, Switzerland LTQ Orbitrap – A Breakthrough Mass Spectrometer for Accurate Mass, High Resolution MS and MSn Analysis on a LC Time Scale
12:30 - 12:40	Closing Remarks

Plenary Lectures

Use of mass spectrometry to study the structure and the interactions of proteins.

Eric Forest CEA/Grenoble Institut de Biologie Structurale (CEA-CNRS-UJF) Laboratoire de Spectrométrie de Masse des Protéines 41 rue Jules Horowitz F-38027 Grenoble Cedex 1 France

In the post-genomic era, the interest in proteins appears again as they execute and control the majority of cellular activities. Through their interactions they play a critical role in cell function or dysfunction.
Characterizing the structure of a protein and the interaction with its partners is a key step in the knowledge of its function and in the use of this protein either as a drug or as a drug target.
Beside the well known role of mass spectrometry (MS) in proteomics, MS can provide useful information in structural biology when associated with other techniques.
For more than ten years the combination of hydrogen exchange and MS has been widely used, providing views on protein structure and protein dynamics. Associating proteolysis with proteases working at low temperature and low pH, local information can be obtained. It enables the identification of the solvent accessible regions of a protein, the location of conformational changes induced by the binding of a partner and the following folding or unfolding of proteins. With the help of directed mutagenesis, it is also possible to finely define the interaction regions with ligands or other proteins.
This method gives structure information in complement to the classical techniques such as NMR or X-ray crystallography. Compared to them, MS offers the advantage of requiring small amounts of sample in conditions close to the physiological ones. Furthermore MS can work much easier on large proteins or complexes.
Several examples illustrating the power of this approach will be given.

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The Quadrupole Ion Trap and Proteomics: New Developments in Top Down and Bottom Up Analysis.

Gary L Glish Department of Chemistry, CB# 3290 University of North Carolina Chapel Hill, NC 27599 USA

While the quadrupole ion trap is already a very powerful and commonly used tool for bottom-up proteomics analysis, performance improvements can be made to increase the information available in these experiments. New methods for CID in the quadrupole ion trap that provide increased sequence coverage, and, in some cases, generate immonium product ions will be presented. Also, a method to increase throughput by analyzing multiple peptide ions simultaneously will be discussed. As a complement to the bottom-up approach, the analysis of intact proteins (top-down) using infrared multiphoton photodissociation will be presented.

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Molecular Electronics: Devices of Tomorrow?

Marcel Mayor Department of Chemistry University of Basel St. Johannsring 19 CH-4056 Basel Switzerland

Institute für Nanotechnologie Forschungszentrum Karlsruhe GmbH PO Box 3640 D-76021 Karlsruhe Germany

Silicon-based integrated circuits have continuously reduced the feature sizes of devices and therewith the cost per functional unit also. However, further decrease in feature size is nowadays becoming increasingly difficult (and expensive) due to physical limitations. Molecular electronics, understood as the integration of molecular structures to supplement specific functionalities on a semiconductor chip, is a promising alternative concept to further reduce both, the feature size and the costs per functional unit. However, currently this remains speculation as the technology to integrate and to address molecules and their assemblies on a chip has not been developed yet. But the strongly increased research activity has already led to some experimental breakthroughs.
Supramolecular chemistry plays a leading role in molecular electronics. Tailor-made molecular devices as potential functional units have already proven to perform specific functions like switching between two configurations triggered by external stimuli. In addition, the integration of molecular structures in electronic circuits crucially depends on the molecules’ supramolecular assembly properties.
An introduction will present the historical background and worldwide current research activities in the field of molecular electronics. Subsequent, own contributions to molecular electronics will be discussed. In particular, investigations to integrate single molecules in electronic circuits and the resulting correlations between molecular structures and electronic transport properties will be presented. The thereby gathered molecular structure vs. electronic conductivity information further allows to design molecular architectures with tailor-made properties, as will be shown by an example of a single molecule rectifier. Further research activities are geared towards molecules with electronic transport properties leading to particular physical properties, like persistent currents or hysteretic switching.
The lecture is focused on the amazing potential of molecular structures to be designed and synthesized to perform particular electronic functions, perhaps even in electronic circuits of tomorrow. However, the fact that this research is still in its infancy and that many innovative ideas and new concepts are still required for the parallel integration of large numbers of molecules or their assemblies will not be hidden.

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Insight into fulvic acid molecules by electrospray mass spectrometry

Decades of research on humic material seemed to confirmed that this kind of natural organic matter was chemically ill-defined and consisted of a seemingly infinite number of unique molecules. It is the merit of electrospray ionization-mass spectrometry that this picture has changes so rapidly in the past years, at least for the very polar fulvic acid fraction of humic material. High resolution mass spectrometry provided the first information on single intact molecules of fulvic acids and offered the potential to investigate these molecules further. Meanwhile molecular formulas of hundreds to thousands of fulvic acid molecules could be determined.
The investigation of fulvic acid isolates by ESI-MS revealed an astonishing degree of regularity at very different levels: (a) periodic intensity distributions were visible in scan spectra recorded by quadrupole-MS, (b) the oligomeric character of fulvic acids of higher molecular weight was detected by size-exclusion chromatography (SEC) -MS analyses and (c) regularities were determined also on the level of elemental composition of fulvic acid molecules by TOF- and FTICR-MS. And finally (d) Q-TOF-MS investigations suggest that also the structure of fulvic acid molecules is very regular. Based on the results obtained by these mass spectrometric methods structure proposals have ben developed for low molecular weight fulvic acids.
With SEC coupled to high resolution MS it is now possible to compare NOM isolates of different origin, to study the reactivity of these molecules and to take up the question of their source materials and formation processes, again. Mass spectrometry may finally enable us to replace the yet only operational definition of fulvic acids by a well defined chemical definition, based on elemental composition and molecular structures.

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