RUHR EXPLORES SOLVATION SCIENCE

RUHR EXPLORES SOLVATION SCIENCE

We shape a new scientific discipline, inspire the scientists of tomorrow, and enable future technologies

WE ARE RESOLV

WE ARE RESOLV

Over 200 scientists from about 50 research groups in 7 institutions

ZEMOS: Home of Solvation Science @RUB

ZEMOS: Home of Solvation Science @RUB

The first research building for Solvation Science in the world. Hosts over 100 scientists, it's home to 6 disciplines.

WHAT is RESOLV?

The Cluster of Excellence RESOLV is a joint research project of about fifty research groups from seven institutions in the German Ruhr area. Since 2012, we use cutting-edge experimental and computational techniques to understand the role of solvents at the molecular detail in the most diverse chemical processes. For example, we investigate the influence of water in vital biological processes as well as the effects of solvents on synthesis and catalytic reactions. Our research lays the foundations for major advances in key green and medical technologies. RESOLV is funded with 28 Mio. EUR by the German Research Foundation (DFG).

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The Bochum Team: Dr. Sergii Shydlovskyi, Dr. Semra Ince and Prof. Dr. Christian Herrmann (from left to right) © RUB, Marquard
A model of hGBP1 function. hGBP1 (top, left in two different representations) reacts with GTP and can follow two competing paths: left) anchoring to a vesicle and subsequent tethering to another vesicle (fluorescence image below); right) polymerization and subsequent disc formation with stacking (electron microscope image below). © Herrmann

#Asktheauthor: How proteins help fight pathogens

3 Questions to RESOLV scientist Christian Herrmann about his recent PNAS publication on hGBP1 mechanism.

1. What is the new discovery that you made?

In the human cell, the Guanylate Binding Protein 1 (hGBP1), is an active player against bacteria and viruses. Yet, its mechanism of action is poorly understood. We found that the function of hGBP1 is controlled by the molecular energy source Guanosine triphosphate GTP. When bound to other molecules (like the monophosphate GMP or the diphosphate GDP), the hGBP1 remains inactive in the cytosol. If hGBP1 binds to GTP, the structure of the protein changes such that the lipid anchor of hGBP1 (a farnesyl group at the C-terminus of hGBP1) becomes available for additional interactions, which depend on the environment. Away from membranes, the protein forms ring-like and cylindrical polymers with the farnesyl groups as a hydrophobic core. In the vicinity of a membrane, the lipid anchor becomes attached to it and further on leads to tethering of near membrane vesicles.

2. What is its significance?

In fighting pathogens, cells act by engulfing bacteria and viruses inside their membrane, forming a vesicle. The new vesicle then tethers and fuses with lysosomes, cellular organelles which provide the necessary enzymes to degrade the pathogen. The mechanism we hypothesized is a central part of the anti-pathogenic activity of hGBP1: We could show that hGBP1 uses the anchor to tether vesicles and could therefore be directly involved in the step before the fusion that leads to pathogen degradation. Based on our findings, in the future it may be possible to elucidate escape strategies of pathogens as well as to gain deeper understanding of specific pathogen defense.

3. Is this related to Solvation Science? If yes, how?

Yes. The lipid anchor switching response is most sensitive to changes of the solvent environment. For example, small changes of the salt concentration change dramatically polymer formation. But even changes in the protein structure (the basis of the molecular switching) are dependent on the salt concentration. In our future studies we want to find out which parts of the protein are responsible to make the system so sensitive to the solvent environment.

Link to RUB press release

Link to original publication

Posted on
The Bochum Team: Dr. Sergii Shydlovskyi, Dr. Semra Ince and Prof. Dr. Christian Herrmann (from left to right) © RUB, Marquard
A model of hGBP1 function. hGBP1 (top, left in two different representations) reacts with GTP and can follow two competing paths: left) anchoring to a vesicle and subsequent tethering to another vesicle (fluorescence image below); right) polymerization and subsequent disc formation with stacking (electron microscope image below). © Herrmann

#Asktheauthor: How proteins help fight pathogens

3 Questions to RESOLV scientist Christian Herrmann about his recent PNAS publication on hGBP1 mechanism.

1. What is the new discovery that you made?

In the human cell, the Guanylate Binding Protein 1 (hGBP1), is an active player against bacteria and viruses. Yet, its mechanism of action is poorly understood. We found that the function of hGBP1 is controlled by the molecular energy source Guanosine triphosphate GTP. When bound to other molecules (like the monophosphate GMP or the diphosphate GDP), the hGBP1 remains inactive in the cytosol. If hGBP1 binds to GTP, the structure of the protein changes such that the lipid anchor of hGBP1 (a farnesyl group at the C-terminus of hGBP1) becomes available for additional interactions, which depend on the environment. Away from membranes, the protein forms ring-like and cylindrical polymers with the farnesyl groups as a hydrophobic core. In the vicinity of a membrane, the lipid anchor becomes attached to it and further on leads to tethering of near membrane vesicles.

2. What is its significance?

In fighting pathogens, cells act by engulfing bacteria and viruses inside their membrane, forming a vesicle. The new vesicle then tethers and fuses with lysosomes, cellular organelles which provide the necessary enzymes to degrade the pathogen. The mechanism we hypothesized is a central part of the anti-pathogenic activity of hGBP1: We could show that hGBP1 uses the anchor to tether vesicles and could therefore be directly involved in the step before the fusion that leads to pathogen degradation. Based on our findings, in the future it may be possible to elucidate escape strategies of pathogens as well as to gain deeper understanding of specific pathogen defense.

3. Is this related to Solvation Science? If yes, how?

Yes. The lipid anchor switching response is most sensitive to changes of the solvent environment. For example, small changes of the salt concentration change dramatically polymer formation. But even changes in the protein structure (the basis of the molecular switching) are dependent on the salt concentration. In our future studies we want to find out which parts of the protein are responsible to make the system so sensitive to the solvent environment.

Link to RUB press release

Link to original publication

Our scientific fields

Research Area A

Understanding and Exploiting Solvation in Chemical Processes

 

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Research Area B

Connecting Solvation Dynamics with Biomolecular Function

 

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Research Area C

Ion Solvation
and Charge Transfer at Interfaces

 

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Video: The solvent of life

Water. It’s the most abundant substance on Earth´s surface and in our bodies. But is water a passive spectator in the animated scene of bio-chemical reactions inside our cells? RESOLV scientists investigate the important role that water plays in the most diverse processes, bringing solvation science into the spotlight.

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The Bochum Team: Dr. Sergii Shydlovskyi, Dr. Semra Ince and Prof. Dr. Christian Herrmann (from left to right) © RUB, Marquard
A model of hGBP1 function. hGBP1 (top, left in two different representations) reacts with GTP and can follow two competing paths: left) anchoring to a vesicle and subsequent tethering to another vesicle (fluorescence image below); right) polymerization and subsequent disc formation with stacking (electron microscope image below). © Herrmann

#Asktheauthor: How proteins help fight pathogens

3 Questions to RESOLV scientist Christian Herrmann about his recent PNAS publication on hGBP1 mechanism.

1. What is the new discovery that you made?

In the human cell, the Guanylate Binding Protein 1 (hGBP1), is an active player against bacteria and viruses. Yet, its mechanism of action is poorly understood. We found that the function of hGBP1 is controlled by the molecular energy source Guanosine triphosphate GTP. When bound to other molecules (like the monophosphate GMP or the diphosphate GDP), the hGBP1 remains inactive in the cytosol. If hGBP1 binds to GTP, the structure of the protein changes such that the lipid anchor of hGBP1 (a farnesyl group at the C-terminus of hGBP1) becomes available for additional interactions, which depend on the environment. Away from membranes, the protein forms ring-like and cylindrical polymers with the farnesyl groups as a hydrophobic core. In the vicinity of a membrane, the lipid anchor becomes attached to it and further on leads to tethering of near membrane vesicles.

2. What is its significance?

In fighting pathogens, cells act by engulfing bacteria and viruses inside their membrane, forming a vesicle. The new vesicle then tethers and fuses with lysosomes, cellular organelles which provide the necessary enzymes to degrade the pathogen. The mechanism we hypothesized is a central part of the anti-pathogenic activity of hGBP1: We could show that hGBP1 uses the anchor to tether vesicles and could therefore be directly involved in the step before the fusion that leads to pathogen degradation. Based on our findings, in the future it may be possible to elucidate escape strategies of pathogens as well as to gain deeper understanding of specific pathogen defense.

3. Is this related to Solvation Science? If yes, how?

Yes. The lipid anchor switching response is most sensitive to changes of the solvent environment. For example, small changes of the salt concentration change dramatically polymer formation. But even changes in the protein structure (the basis of the molecular switching) are dependent on the salt concentration. In our future studies we want to find out which parts of the protein are responsible to make the system so sensitive to the solvent environment.

Link to RUB press release

Link to original publication

gss summer school

The Graduate School Solvation Science hosts an annual Summer School at the Ruhr University Bochum. The school always takes place during Whitsuntide and is an integral part of the GSS students' training during their doctoral studies. The fourth GSS Summer School took place from the 6th to the 9th of June, 2017.

International speakers, suggested by the students themselves, are invited to give keynote talks on their research in the field of Solvation Science. The Advanced Laboratory Modules give the students an excellent opportunity to learn new and interesting experimental and theoretical techniques within a specific research topic of their own choice. In 2017 the program of the Summer School comprised a career day, in addition.

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Publications highlight

T. Schleif, J. Mieres-Perez, S. Henkel, M. Ertelt, W. T. Borden, W. Sander
The Cope Rearrangement of 1,5-Dimethylsemibullvalene-2(4)-d1: Experimental Evidence for Heavy-Atom Tunneling
Angew. Chem. 129 (2017), 10886
DOI: 10.1002/ange.201704787 

K. F. Pfister, S. Baader, M. Baader, S. Berndt, L. J. Goossen
Biofuel by isomerizing metathesis of rapeseed oil esters with (bio)ethylene for use in contemporary dieses engines
Science Advances  3 (2017),  e1602624
DOI: 10.1126/sciadv.1602624

C. Schuabb, N. Kumar, S. Pataraia, D. Marx, R. Winter
Pressure modulates the self-cleavage step of the hairpin ribozyme
Nature Communications 8 (2017), 14661
DOI: 10.1038/ncomms14661

 

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