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Structure and dynamics of intermediate states in protein folding

Objectif



Young postdoctoral researchers will be given the opportunity to apply all countries, cooperating to study the intriguing, but elusive mechanism of the available techniques to the particular protein, or class of proteins, protein folding. Two of the groups have a strong background in that was assigned to them. We foresee that at least some of these trainees computational biophysics, the remaining groups are equipped to do will actually perform part of their research in other laboratories within experimental work on various proteins. The combined expertise includes the network. They will be trained, not only to apply these techniques, but also to cooperate closely with theoreticians, working on the same protein, important techniques like NMR and mass spectrometry, as well as stopped flow spectroscopy, calorimetry, and molecular biology, peptide synthesis to formulate testable models of protein folding and to perform protein engineering. From the theoretical point of view we envisage an evaluate such tests. On the other hand, theoreticians will be trained in important role for molecular dynamics calculations in combination with the producing testable models wherever possible, and to accommodate the results essential dynamics analysis.
of such tests in an improved model. They will be encouraged to participate The primary issue will be the identification, by theoretical and in network research meetings, network discussions (possibly via the experimental means, of nucleation centres, where protein folding is Internet), as well as the regular summer schools, master classes, and initiated, and of folding intermediates, followed by their structural and international conferences.
kinetic characterisation. Where possible stable nucleation centres and folding intermediates will be prepared in isolation, by synthesis or via expression of the corresponding genes in microorganisms, for more detailed structural studies and kinetic measurements. In parallel computer models will be studied, with an emphasis on the correct modelling of solvent/solute interactions, in order to formulate testable hypotheses of the sequence of events in protein folding and the nature of nucleation centres and folding intermediates.

Thème(s)

Appel à propositions

Data not available

Régime de financement

NET - Research network contracts

Coordinateur

NETHERLANDS RESEARCH SCHOOL FOR ASTRONOMY - LEGALLY REPRESENTED BY UNIVERSITY OF GRONINGEN
Contribution de l’UE
Aucune donnée
Adresse
4,Nijenborgh 4
9747 AG GRONINGEN
Pays-Bas

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Coût total
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Participants (6)