Towards unidirectional reconstitution of membrane proteins into liposomes.

Amati, Andrea Marco; Schär, Sandra; von Ballmoos, Christoph (27 August 2017). Towards unidirectional reconstitution of membrane proteins into liposomes. (Unpublished). In: 1st International Conference of Molecular Systems Engineering. University of Basel, Switzerland. 27.-29.08.2017.

For functional studies, membrane proteins (MPs) are often purified and integrated (reconstituted) into systems which mimic their natural environment in a membrane as e.g. liposomes, allowing to investigate its function and structural aspects without any disturbing background from their native environment. The most important problem during MP-reconstitution is the often random orientation of the MP in the liposomal membrane after reconstitution. For functional studies of the MP of interest and quantitative analysis of its properties, unidirectional orientation in the liposomal membrane is required. Previous work of other groups did not include a final and universal approach and procedures have to be individually optimized for an enrichment of enzyme orientation. In most cases, however, orientation cannot be influenced and is thought to depend on the 3D structure of the protein. We are currently developing and establishing a universal method to force unidirectional reconstitution of MPs by the aid of a molecular unit that can be attached to every protein. Once our method is fully established, the interplay of two or more membrane proteins can be investigated more quantitatively.

Item Type:

Conference or Workshop Item (Poster)

Division/Institute:

08 Faculty of Science > Departement of Chemistry and Biochemistry

Graduate School:

Graduate School for Cellular and Biomedical Sciences (GCB)

UniBE Contributor:

Amati, Andrea Marco; Schär, Sandra and von Ballmoos, Christoph

Subjects:

500 Science > 570 Life sciences; biology
500 Science > 540 Chemistry

Language:

English

Submitter:

Andrea Marco Amati

Date Deposited:

16 Oct 2017 09:10

Last Modified:

16 Oct 2017 09:10

URI:

https://boris.unibe.ch/id/eprint/105234

Actions (login required)

Edit item Edit item
Provide Feedback