Research Highlights chair op Physical Chemistry II

Physical Chemistry II - Laser spectroscopy and Biophotonics

Ein Gefrierschutzprotein aus dem Blut von Fischen verändert die Wassermoleküle in seiner Umgebung so, dass ihnen nicht das Blut in den Adern gefriert.
TV review 3sat/Nano 31th March 2011 (german)

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Antifreeze glycoprotein activity correlates with long-range protein-water dynamics

S. Ebbinghaus, K. Meister, B. Born, A. L. DeVries, M. Gruebele, M. Havenith

Communication, Journal of the American Chemical Society. August 16, 2010, DOI: 10.1021/ja1051632

Press Release: Frostschutz bei Fischen
Artikelin "Die Zeit" from 26.8.2010, Nr. 35, S. 36 (2010)

Interview
Secrets of anti-freeze proteins in Antarctic fish unlocked

Download the full interview here

Press Release: Anti-Freeze-Protein beeinflusst die Bewegung umgebender Wassermolekühle" "Press release Ruhr-University Bochum

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Label-Free Imaging of Metal-Carbonyl Complexes in Live Cells by Raman Microspectroscopy

K. Meister, J. Niesel, U. Schatzschneider, N. Metzler-Nolte, D. A. Schmidt, M. Havenith
Angewandte Chemie International Edition 49, 3310-3312 (2010). Supporting Material

Press Release: "Good vibrations" help in research into new bioactive metal complexes - RUB researchers study their intracellular distribution in living cancer cells - "VIP" publication in the professional journal "Angewandte Chemie"

Highlight from P. Hildebrandt
A Spectral Window to the Cell
Angewandte Chemie Int. Ed. 2010, 49 DOI: 10.1002/anie.201001616

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Press release : Observation: Formation of the smallest droplet of acid

06/2009: Press release
- New reaction mechanism at ultracold temperatures - Chemists in Bochum report in Science: 4 water molecules and one HCl are enough

Exactly four water molecules and one hydrogen chloride molecule are necessary to form the smallest droplet of acid. This was the result of work by the groups of Prof. Dr. Martina Havenith(physical chemistry) and Prof. Dr. Dominik Marx (theoretical chemistry) within the research group FOR 618. They have carried out experiments at ultracold temperatures close to absolute zero temperature using infrared laser spectroscopy to monitor the molecules. This has been accompanied by theoretical ab initio simulations. According to their calculations, the reaction at these extremely cold temperatures is only possible if the molecules are aggregating one after the other. Their results will be published in the newest issue of “Science”.

Science Article
A. Gutberlet, G. Schwaab, Ö. Birer, M. Masia, A. Kaczmarek, H. Forbert, M. Havenith, D. Marx
Aggregation-Induced Dissociation of HCl(H2O)4 below 1 K: The Smallest Droplet of Acid
Science 324, 1545-1548 (2009). DOI: 10.1126/science.1171753 - Supporting Material.

Nature Research Highlight in Chemistry
The tiniest acid drop
Nature 459, 1036 (25 June 2009). DOI: 10.1038/4591036d

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Press release :Topographie und Chemie von Nanotexten

05/2008: Press release
Topographie und Chemie von Nanotexten
New combined microscope allows reading and writing awards in two ways with RUB-chemistry poster prize.

Image Information: Nano-Smiley - In a HS-C6H12-OH monolayer was written with single-stranded DNA a face. The line width is 50 nm

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Press release : Protein Folding Modifies the Water in the Environment

02/2008: Press release
Protein Folding Modifies the Water in the Environment - New Knowledge Gained From Terahertz Spectroscopy - RUB Chemistry Observes “THz Dance“ Changes

Just a few weeks ago, teams from Bochum, Illinois, and Nevada were able to prove with terahertz (THz) spectroscopy that proteins do modify water molecules in their environment to a long range extent: The water molecules, which generally move around like disco dancers in their collective network motions behave more like in a neat minuet under protein influence. The group by Prof. Dr. Martina Havenith-Newen (Physical Chemistry II Dpt., RUB) managed to find out more about the rules of this dance. They could show that protein folding changes the dancing steps of the water. A partly unfolded protein will affect water molecules within the dynamical hydration shell to a much less extent than a folded one does. The higher the flexibility of the protein, the less affected is the water. The scientists present their conclusions as a “communication“ in the Journal of the American Chemical Society.

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Press release : The terahertz dance of water with proteins

12/2007: Press release
The terahertz dance of water with proteins - PNAS reports: Disco becomes a minuet - Protein influence has a previously unsuspected long reach

It is in particular the type of fold that determines the function of proteins – this is a dynamic process that takes place very quickly. Up to now, the investigation of this protein "dance" has ignored its dancing partner: Water. This interplay between water and proteins has now been observed using terahertz spectroscopy by researchers from Bochum, Illinois und Nevada under the guidance of Prof. Dr. Martina Havenith-Newen (Physical Chemistry II at the RUB). This has enabled them to demonstrate for the first time that proteins influence the movements of the surrounding water network over a broad area. Some 1000 water molecules are "brought into line" by one protein: If their movement without protein more closely resembles a bunch of unchoreographed disco dancers, then in the vicinity of a protein it looks more like they are dancing a minuet. The researchers report on their study in the current edition of the Proceedings of the National Academy of Science PNAS.

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Press release : Der Terahertz-Tanz des Wassers mit den Proteinen

12/2007: Press release
Der Terahertz-Tanz des Wassers mit den Proteinen - PNAS berichtet: Disko wird zum Menuett - Protein-Einfluss hat eine unvermutet große Reichweite

It is particularly the type of fold that determines the function of proteins - a dynamic process that takes place very quickly. An examination of this "dance" of the proteins we have so far ignored the partner: water. This interplay between water and proteins, researchers from Bochum, Illinois and Nevada to Prof. Dr. Martina Havenith-Newen (Physical Chemistry II RUB) is now observed with terahertz spectroscopy. They were the first to show that proteins influence the movements of the surrounding water network over wide areas. Some 1000 water molecules are "brought into line" by a protein: Do they move without protein so muddled as a group of disco dancers, then they go in the vicinity of a protein rather than a minuet. The researchers report their study in the current issue of Proceedings of the National Academy of Science PNAS.

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Press release : Mit Terahertzstrahlung uraltes Rätsel gelöst

08/06 Press release
Mit Terahertzstrahlung uraltes Rätsel gelöst - Wasser ist aktiv: RUB-Chemiker beenden Spekulationen

Image: Wasser Moleküle innerhalb einer Solvatationsschale von 4 Ångström um ein Laktosemolekül.
Basis ist ein Schnappschuss eines CHARMM Moleküldatensatzes (D. Leitner) grafisch aufgearbeitet (E. Bründermann).

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