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Integral membrane proteins resolution of stoichiometry and structure

Our recent discovery, that large integral membrane protein complexes can survive intact in the mass spectrometer, prompts many new experiments to understand the mechanism of their release from micelles and to maximise the impact o... ver más

31/05/2016

UOXF

2M€

Presupuesto del proyecto: 2M€

Líder del proyecto

THE CHANCELLOR MASTERS AND SCHOLARS OF THE UN... No se ha especificado una descripción o un objeto social para esta compañía.

TRL 4-5

Fecha límite participación Sin fecha límite de participación.

Financiación concedida El organismo FP7 notifico la concesión del proyecto el día 2016-05-31 No tenemos la información de la convocatoria

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Líder del proyecto

THE CHANCELLOR MASTERS AND SCHOLARS OF THE UN... 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 Our recent discovery, that large integral membrane protein complexes can survive intact in the mass spectrometer, prompts many new experiments to understand the mechanism of their release from micelles and to maximise the impact of this finding. We propose to examine the structure of membrane complexes after their release from micelles in the gas phase. We will apply ion mobility mass spectrometry to extract collision cross sections of membrane complexes of known structure and compare these with those calculated form atomic coordinates. Conditions will be optimised to minimise the distortion of structure. More controlled release of membrane complexes from micelles will be investigated using photo-activation. To do this we will explore properties of detergents incorporating chromophores, with infra red laser activation to activate the micelle selectively without perturbing the membrane protein complex. We also propose to develop methods for determining structures of lipids bound specifically in membrane protein interfaces and assess their effects on the stability and stoichiometry of the complex. To visualise these complexes in the absence of micelles we propose to 'soft land' membrane protein complexes on electron microscopy grids, targeting components by virtue of their mass to charge. We will apply these methods to some of the most challenging and controversial membrane protein complexes including EmrE, the intact ATP synthases, the M2 proton channel of the influenza A virus, the P-type ATPases and the ATP-sensitive potassium channel. Overall, through this ambitious program of research, we plan to shed new light on membrane protein complexes and the role of lipids and small molecules in stabilising and modifying their properties.

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