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Contenu archivé le 2022-12-23

The dynamics of protein structure

Objectif



Protein molecules are highly flexible and can assume a large number of structurally slightly different states, called conformational substates. At physiological temperatures a molecule fluctuates among these conformational substates. Reducing the temperature the fluctuations die out at a critical temperature which is comparable to a glass transition. In proteins this critical temperature is at about 200K. The two additonal proposals from Estonia and Hungaria extend the original project in the following way: Optical spectroscopy is used in order to understand the inset of protein dynamics around the glass transition. Below the glass transtion the structural distributions are investigated by hole burning. Temperature Derivative Spectroscopy will be used to follow structural rearrangements after photoreactions. These spectroscopic methods have not been included into the original proposal. Besides of investigations on myoglobin, bacteriorhodopsin and the reaction center from photosynthetic bacteria are in the centre of interest of the additional proposals.

Appel à propositions

Data not available

Régime de financement

CSC - Cost-sharing contracts

Coordinateur

Technische Universität München
Contribution de l’UE
Aucune donnée
Adresse
James-Franck-Straße
85748 Garching bei München
Allemagne

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Coût total
Aucune donnée

Participants (2)