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Multi protein interaction kinetics by single molecule methods

Objective of this proposal is to obtain a real time picture of how components of a multi-protein complex interact to perform complex regulated tasks, in particular to see how a protein system might be more than the sum of its comp... ver más

30/09/2021

ALU-FR

2M€

Presupuesto del proyecto: 2M€

Líder del proyecto

ALBERTLUDWIGSUNIVERSITAET FREIBURG No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Fecha límite participación Sin fecha límite de participación.

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Financiación concedida El organismo H2020 notifico la concesión del proyecto el día 2021-09-30

ERC-CoG-2015: ERC Consolidator Grant

I+D

Cerrada hace 9 años

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No hay información privada compartida para este proyecto. Habla con el coordinador.

2 Participantes

ALU-FR

1.88M€ | Lider

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Duración del proyecto: 67 meses Fecha Inicio: 2016-02-02
Fecha Fin: 2021-09-30

Líder del proyecto

ALBERTLUDWIGSUNIVERSITAET FREIBURG No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Presupuesto del proyecto 2M€

Fecha límite de participación Sin fecha límite de participación.

Descripción del proyecto Objective of this proposal is to obtain a real time picture of how components of a multi-protein complex interact to perform complex regulated tasks, in particular to see how a protein system might be more than the sum of its components. In living organisms many proteins work in complexes to form multicomponent protein machines and to regulate cellular processes. The function of such multicomponent machines is usually addressed by dividing them into a collection of two state systems at equilibrium. Many molecular machines work in large complexes with multiple states out of equilibrium by utilizing the energy of ATP hydrolysis. In this proposal the real time kinetics of multi-protein interactions in and out of equilibrium will be investigated using single molecule methods. The succession of association and dissociation steps as well as large conformational changes within the proteins will be monitored simultaneously with multicolour single molecule FRET in real time. In order to observe at the same time the folding state of proteins, a combination of optical tweezers and single molecule FRET will be developed. Finally, a combination of microfluidics for fast mixing and single pair FRET will be developed to investigate interactions of low affinity. A large part of the experiments will focus on the example of the heat shock protein Hsp90 system, which consists of co-chaperones, clients and nucleotides. Altogether, these interdisciplinary experiments will yield unprecedented information on multi-component interactions in equilibrium and out of equilibrium on timescales from sub milliseconds to hours. I am confident that these studies will have an impact on the understanding of the Hsp90 machinery as well as general principles of multi-component protein systems, which is the basis for understanding cellular processes.

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