Published in
Royal Society of Chemistry, Nanoscale, 31(13), p. 13519-13528, 2021
DOI: 10.1039/d1nr02419a
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Differences in SMA-like polymer architecture dictate the conformational changes exhibited by the membrane protein rhodopsin encapsulated in lipid nano-particles
Journal article published in 2021 by
Rachael L. Grime 
,
Richard T. Logan ,
Stephanie A. Nestorow,
Pooja Sridhar,
Patricia C. Edwards ,
Christopher G. Tate,
Bert Klumperman ,
Tim R. Dafforn,
David R. Poyner ,
Philip J. Reeves,
Mark Wheatley
,
Richard T. Logan ,
Stephanie A. Nestorow,
Pooja Sridhar,
Patricia C. Edwards ,
Christopher G. Tate,
Bert Klumperman ,
Tim R. Dafforn,
David R. Poyner ,
Philip J. Reeves,
Mark Wheatley
This paper was not found in any repository, but could be made available legally by the author.
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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.