Lennart B.-Å. Johansson: Polarised light spectroscopy and energy migration/transfer with applications in biosciences
The project aims at a molecular-level-development of polarised light spectroscopy for insights into complex biostructures, in particular the dynamics, structure and functioning of proteins related to e.g. the folding and formation of regular protein aggregates (= non-covalent polymers).
A new approach to the theoretical description and experimental studies of bio-macromolecular structures is used, which is based on electronic energy transport between chemically identical or different fluorescent groups. These extrinsic or intrinsic groups are localised at specific positions, e.g. in a protein structure. Time-resolved polarised fluorescence spectroscopic experiments are applied in studies of these groups in the absence and presence of energy transport. The energy migration/transfer among fluorophores is described within a recently developed extended Förster theory (EFT), which brings the theoretical analysis of experimental data to the same level of molecular detail as in ESR and NMR spectroscopy. The EFT involves stochastic equations, which necessitate the use of Brownian dynamics simulations.
In another branch of the project, fundamental aspects of enhanced one-photon and two-photon excited fluorescence are studied. Potential applications of these processes are, for instance as amplifiers of chemical sensors.
OPEN: PhD student position
Fluorescence spectroscopy & extended Förster theory development with applications to structure-function studies of proteins
In the PhD project, time-resolved fluorescence depolarisation experiments are performed and analysed by means of ongoing and recent theoretical advancements of electronic energy transfer. Applications of computational methods (e.g. Brownian dynamics simulations) are crucial. The project aims at:
- applying currently developed methods for the determination of structure and structural changes of globular proteins (e.g. protein folding), as well as regular protein aggregates (e.g. amyloid and fibril structures)
- a continuing development of extended Förster theory and its testing on synthetic and experimental data obtained by one- as well as two-photon excited fluorescence. Time-resolved fluorescence data are recorded by using the single-photon counting technique.
The project involves interdisciplinary collaborations with theoretical chemists, biochemists, medical chemists as well as plant physiologists at Umeå University.
For more information, please contact Prof. Lennart B.-Å. Johansson: Phone +46-(0)90-786 51 49; Cell phone +46 702122521; E-mail: email@example.com