Differences in SMA-like polymer architecture dictate the conformational changes exhibited by the membrane protein rhodopsin encapsulated in lipid nano-particles

Author:

Grime Rachael L.12ORCID,Logan Richard T.1,Nestorow Stephanie A.1,Sridhar Pooja1,Edwards Patricia C.3ORCID,Tate Christopher G.3,Klumperman Bert4ORCID,Dafforn Tim R.1,Poyner David R.5,Reeves Philip J.6,Wheatley Mark72ORCID

Affiliation:

1. School of Biosciences, University of Birmingham, Birmingham, B15 2TT, UK

2. Centre of Membrane Proteins and Receptors (COMPARE), University of Birmingham and University of Nottingham, Midlands, UK

3. MRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 0QH, UK

4. Department of Chemistry and Polymer Science, Division of Polymer Science, Stellenbosch University, Private Bag X1, Matieland 7602, South Africa

5. Life and Health Sciences, Aston University, Birmingham B4 7ET, UK

6. School of Life Sciences, University of Essex, Wivenhoe Park, Essex CO4 3SQ, UK

7. Centre for Sport, Exercise and Life Sciences, Institute for Health & Wellbeing, Alison Gingell Building, Coventry University, Coventry, CV1 2DS, UK

Abstract

Using the GPCR rhodopsin as an exemplar, SMA SMI and DIBMA constitute a ‘tool-kit’ of structurally-related solubilising polymers, with each providing different advantages for studying membrane proteins encapsulated in lipid particles.

Funder

Biotechnology and Biological Sciences Research Council

Medical Research Council

Department of Science and Innovation, South Africa

National Research Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

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