Professor Martina Havenith, Institute for Physical Chemistry, Ruhr-University Bochum
Seminar |Tuesday, September 23 | 11 a.m.-12 p.m. | 775 Tan Hall
There is a vast body of literature that considers solvents as inert media for molecular processes.Transcending this traditional view, solvents are now increasingly recognized as playing an active role in their own right. Recent advances in investigative techniques and theory now make possible new approaches to probing, describing, and influencing structure, dynamics, and kinetics of complex solvation phenomena at the molecular level. Solvation Science will provide a unifying framework for understanding and predicting solvent processes. We could shown that THz absorption spectroscopy in combination with MD simulations is providing a sensitive tool to probe subtle changes in hydration dynamics caused by a solute.
Salts are known to show highly ion-specific, stabilizing or destabilizing effects on the thermal and functional stability of proteins. The direction and magnitude of these effects obey universal anion and cation series, known as Hofmeister series. Albeit ion solvation is of central importance in chemistry (from atmospheric to biochemistry), a full molecular description is still a subject of controversial debates. We have carried out a systematic terahertz absorption spectroscopy and molecular dynamics simulation study of a series of aqueous solutions of mono-, divalent, and trivalent salts, which adds a new piece to the controversy of long range versus short range interactions.
In life science water is the ubiquitous solvent, sometimes even called the “matrix of life”. There are more and more experimental and theoretical evidences that solvation water is not a passive spectator in biomolecular processes. Our studies revealed that an efficient dynamical coupling of the THz dynamics of biomolecules with those of their hydration shells can play a key role in biomolecular mechanisms. A two-tier (short-range and long-range) solute-solvent interaction together with a heterogeneous hydration dynamics towards functional sites appear to be fundamental elements of this coupling. We propose that this gradient of water motions, the so-called “hydration funnel” is playing a -so far neglected- role in molecular recognition.
References:
Grossmann, Born, Heyden, Tworowski, Fields, Sagi, Havenith, Correlated structural kinetics and retarded solvent dynamics at the metalloprotease active site, Nature Structural & Molecular Biology 18, 1102-1108 (2011).
Funkner, Niehues, Schmidt, Heyden, Schwaab, Callahan, Tobias, Havenith, Watching the low frequency motions in aqueous salt solutions – the terahertz vibrational signatures of hydrated ions, JACS, 134, 1030-1035 (2012).
Meister, Ebbinghaus, Xu, Duman, DeVries, Gruebele, Leitner, Havenith, Long-range protein-water dynamics in hyperactive insect antifreeze proteins, Proc. Natl. Acad. Sci. USA 110(5) 1617-1622 (2013).
Conti Nibali, Havenith, New Insights into the Role of Water in Biological Function: Studying Solvated Biomolecules Using Terahertz Absorption Spectroscopy in Conjunction with Molecular Dynamics Simulations, JACS dx.doi.org/10.1021/ja504441h (2014)
Salts are known to show highly ion-specific, stabilizing or destabilizing effects on the thermal and functional stability of proteins. The direction and magnitude of these effects obey universal anion and cation series, known as Hofmeister series. Albeit ion solvation is of central importance in chemistry (from atmospheric to biochemistry), a full molecular description is still a subject of controversial debates. We have carried out a systematic terahertz absorption spectroscopy and molecular dynamics simulation study of a series of aqueous solutions of mono-, divalent, and trivalent salts, which adds a new piece to the controversy of long range versus short range interactions.
In life science water is the ubiquitous solvent, sometimes even called the “matrix of life”. There are more and more experimental and theoretical evidences that solvation water is not a passive spectator in biomolecular processes. Our studies revealed that an efficient dynamical coupling of the THz dynamics of biomolecules with those of their hydration shells can play a key role in biomolecular mechanisms. A two-tier (short-range and long-range) solute-solvent interaction together with a heterogeneous hydration dynamics towards functional sites appear to be fundamental elements of this coupling. We propose that this gradient of water motions, the so-called “hydration funnel” is playing a -so far neglected- role in molecular recognition.
References:
Grossmann, Born, Heyden, Tworowski, Fields, Sagi, Havenith, Correlated structural kinetics and retarded solvent dynamics at the metalloprotease active site, Nature Structural & Molecular Biology 18, 1102-1108 (2011).
Funkner, Niehues, Schmidt, Heyden, Schwaab, Callahan, Tobias, Havenith, Watching the low frequency motions in aqueous salt solutions – the terahertz vibrational signatures of hydrated ions, JACS, 134, 1030-1035 (2012).
Meister, Ebbinghaus, Xu, Duman, DeVries, Gruebele, Leitner, Havenith, Long-range protein-water dynamics in hyperactive insect antifreeze proteins, Proc. Natl. Acad. Sci. USA 110(5) 1617-1622 (2013).
Conti Nibali, Havenith, New Insights into the Role of Water in Biological Function: Studying Solvated Biomolecules Using Terahertz Absorption Spectroscopy in Conjunction with Molecular Dynamics Simulations, JACS dx.doi.org/10.1021/ja504441h (2014)
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