The membrane protein LeuT in micellar systems: aggregation dynamics and detergent binding to the S2 site.

ABSTRACT: Structural and functional properties of integral membrane proteins are often studied in detergent micellar environments (proteomicelles), but how such proteomicelles form and organize is not well understood. This makes it difficult to evaluate the relationship between the properties of the proteins measured in such a detergent-solubilized form and under native conditions. To obtain mechanistic information about this relationship for the leucine transporter (LeuT), a prokaryotic homologue of the mammalian neurotransmitter/sodium symporters (NSSs), we studied the properties of proteomicelles formed by n-dodecyl-β,D-maltopyranoside (DDM) detergent. Extensive atomistic molecular dynamics simulations of different protein/detergent/water number ratios revealed the formation of a proteomicelle ch

SUBMITTER: Khelashvili G 

PROVIDER: S-EPMC3788620 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature