Sunday, 28 March
|
|
Opening of conference
|
|
Plenary lecture 1:
|
|
7.20 |
Opening of Poster Session (All Numbers)
Opening Reception and Banquet |
Monday, 29 March
|
I.
New Methods in FTMS
|
|
|
|
|
L2: M. Linscheid, S. Beck, T. Hagemeister, and V. Livadaris
Humboldt Universität zu Berlin, Germany
Fourier-Transform Mass Spectrometry Using the Finnigan LTQ FTMS - High
Resolution - High Accuracy as Analytical Routine |
|
L3: J. Pittman, B. Thomson, and P. O'Connor
Boston University School of Medicine, USA
A New Hybrid ESI-qQq FTMS |
10.40 |
Break |
II.
Bioanalytical Applications A |
|
|
|
|
L5: M. Mormann, L. Bindila, M. Froesch, A. Zamfir, and J.
Peter-Katalinić
University of Münster, Germany
FT-ICR MS of Complex Carbohydrates |
|
L6: C. Hendrickson, G. Blakney, M. Chalmers, L. Mackay,
M. McFarland, J. Quinn, and A. Marshall
Florida State University, USA
Instrumental Advances in FT-ICR MS/MS of Biomolecules |
12.50 |
Lunch break |
1.00 |
Poster Session (A)
(odd numbers) |
III.
Fundamentals |
|
|
|
|
L8: K. Wanczek and K. Garbade
University of Bremen, Germany
Understanding Ion-Ion Reactions in the Gas Phase |
|
L9:
I.
Balteanu.
P. Balaj, B. Fox-Beyer, M. Beyer, V. Bondybey
Technische Universität München, Germany
Use of Isotopically Enriched Material in Gas Phase Cluster Studies |
|
Break |
IV.
Spectroscopy and Atomic Clusters |
|
|
|
|
L11: L. MacAleese, J. Lemaire, J.-M. Ortega, and P. Maître
University of Paris, France
Infrared Spectroscopy Under FT-ICR-MS Conditions : Experimental Setup and
Applications to Organometallics |
|
L10: L. Schweikhard, K. Blaum, A. Herlert, G. Marx
Ernst-Moritz-Arndt-Universität, Greifswald, Germany
Atomic Clusters and Ion Cyclotron Resonance Mass Spectrometry – A
Fruitful Combination |
|
Guided tours:
Walls tell tales
Popes, heretics, courtesans |
Tuesday, 30 March
|
V.
New Methods and Instrumentation
|
|
|
|
|
L14: W. Metelmann-Strupat, K. Strupat, J. Griep-Raming, and
H. Münster
Thermo Electron, Bremen, Germany
Accurate Mass and High Scan Speed – Using Two Detectors in One
Instrument |
|
L15: D. Davis, K. Gallaher, W. Rimkus
Siemens Applied Automation, Bartlesville, USA
Use of a Miniature High Resolution Fourier Transform – Mass
Spectrometer for Support of Product and Process Analysis |
10.30 |
Break |
VI.
New
Bioanalytical Methods |
|
|
|
|
L17: M. Allen A. Sterling, and M. Baumert
Advion BioSciences, Norwich, UK
Fully Automated High Throughput Analysis Using Chip-Based Nanoelectrospray
FT-ICR Mass Spectrometry |
|
L18: C. Hagman, M. Ramström, P. Håkansson, J. Bergquist
Uppsala University, Sweden
Quantitative Analysis of Tryptic Protein Mixtures Using Electrospray
Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry |
12.40 |
L19: R. Geels,
A. Heck, S. van der Vies,
and
R. Heeren
FOM- Institute for Atomic and Molecular Physics, Amsterdam,
The Netherlands
Dissociation Analysis of GroES via SORI-CID in an FT‑ICR‑MS |
1.10 |
Lunch break |
VII.
Dissociation Techniques |
|
L20: C. Adams, B. Budnik, K. Haselmann, F. Kjeldsen, and R. Zubarev
Uppsala University, Sweden
Electron Capture Dissociation Detects the Presence of a Single D‑Amino
Acid in a Protein and Probes the Neutral Tertiary Structure |
G.
Baykut |
|
L21: K. Breuker and Fred W. McLafferty
University of Innsbruck, Austria
Native Electron Capture Dissociation |
|
L22: H. Cooper
University of Birmingham, England
Electron Capture Dissociation of Non-Standard and Modified Peptides |
3.40 |
L23: Y. Tsybin, M. Witt, G. Baykut, G. Weiss, P. Håkansson
University Uppsala, Sweden
Optimization of ECD: Mechanistic Studies, Top-Down and Bottom-Up
Applications |
4.10 |
Break |
VIII.
Bioanalytical Applications B |
4.40 |
L24: M. Freitas and L. Zhang
Ohio State University, USA
Cracking the Histone Code: A Mass Spectrometry Based Approach for the
Determination of Histone Modifications |
M.
Linscheid |
5.10 |
L25: M. Ramström, I. Ivonin, A. Johansson, H. Askmark, K. E.
Markides, R. Zubarev, P. Håkansson, S.-M. Aquilonius, and J. Bergquist
Uppsala University, Sweden
Protein Patterns in Cerebrospinal Fluid Revealed by Liquid
Chromatography Fourier Transform Ion Cyclotron Resonance Mass Spectrometry |
5.40 |
L26: A. Sinz, D. Schulz, C. Ihling, S. Kalkhof, and M. Clore
University Leipzig, Germany
Mapping Protein Interfaces by Chemical Cross-Linking and FTICR Mass
Spectrometry: Application to Calmodulin/Peptide Complexes |
6.10 |
L27 X. Tian, R. Cecal, J. McLaurin, R. Stefanescu, M. Manea,
S. Grau, M. Ehrmann, P. St George-Hyslop, and M. Przybylski
University of Konstanz, Germany
Application of FTICR-MS in Characterisation of Target Peptides/Proteins
of Alzheimer's Disease and Elucidation of an Amyloid Plaque-Specific
Epitope |
6.40 |
Departure:
Guided tour of Joh. Albrecht Brewery with evening meal
Wine Tasting in the Spitalkellerei Konstanz |
Wednesday, 31 March
|
IX.
New FTMS
Methods |
|
|
|
|
L29: P. O'Connor
Boston University School of Medicine, USA
Current Thoughts Regarding the Cryogenic FTMS |
|
L30: V. Frankevich, X. Guan, M. Dashtiev, and R. Zenobi
Swiss Federal Institute of Technology (ETH),
Zurich, Switzerland
Laser-Induced Fluorescence of Trapped (Bio)Molecular Ions |
10.40 |
Break |
X.
Analytical Applications |
|
|
|
|
L32: A. Stopford, N. Polfer, P. Langridge-Smith
University of Edinburgh, Scotland
A Study of Electron Capture Dissociation Efficiency of Peptide
Dications Using a Dispenser Cathode |
|
L33: T. Bristow
LGC, Teddington, England
A Comparison of Calibration Methods for Accurate Mass Measurement of
Low Molecular Weight Molecules Using FTMS |
12.40 |
Lunch break |
1.00 |
Poster Session B (even numbers) |
Ceremonial Act in Honour of the Scientific Career of
Jean Futrell and Burnaby Munson
|
|
Honorary address:
G. von Graevenitz, Rector, University of Konstanz
P.
Derrick:
Laudatio on Jean Futrell
F. McLafferty: Laudatio on Burnaby Munson
Award of special EJMS Issue |
|
|
Honorary Lecture:
Jean Futrell, Pacific Northwest National Laboratory, Richland, USA
Kinetics of Activation and Dissociation of Large Molecular Ions in the
Gas Phase |
F.
McLafferty |
|
Honorary Lecture:
Burnaby Munson,
University of Delaware, USA
Chemical Ionization Mass Spectrometry: A Useful Accident |
M.
Przybylski |
|
Break |
|
Plenary lecture 2:
H.
Schwarz,
Technische Universität Berlin, Germany
Elementary Processes in Catalysis:Looking at and Learning from "Naked"
Transition. Metal Ion Chemistry and Physics – Theory and Experiment in
Concert |
A.
Marshall |
5.00 |
Departure to Meersburg Castle and Conference Dinner |
Thursday, 1 April
|
XI.
Perspectives for FTMS |
|
|
|
|
L35: B. Paizs, M. Schnölzer, U. Warnken, and S. Suhai
German Cancer Research Center, Heidelberg, Germany
Ion Intensity Relationships for the MS/MS Spectra of Protonated Peptides |
|
L36: C. Koy, P. Serrano, S. Möller, B. Ringel, S. Mikkat, R. Martin,
S. Drynda, J. Kekow, H.-J. Thiesen, and M. Glocker
Proteome Center Rostock, Germany
Identification and Structure Characterization of Disease-Associated
Marker Proteins Using MALDI QIT ToF MSn in Clinical Proteome Research with
Patients Suffering from Rheumatoid Arthritis |
10.30 |
Break |
XII.
Bioanalysis Highlights in FTMS |
|
|
|
|
Awards |
|
Plenary lecture 3:
F.
McLafferty,
Cornell University, Ithaca, USA
Structural Characterization of Biomolecules, Unique Advantages of FTMS |
M.
Przybylski |
13.10 |
Closing remarks and end of conference |