id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-299270-fwbz3t25	Lemieux, M. Joanne	Structure and function of proteins in membranes and nanodiscs	2020-08-22		.txt	text/plain	3034	145	39	Abstract The field of membrane structural biology represents a fast-moving field with exciting developments including native nanodiscs that allow preparation of complexes of post-translationally modified proteins bound to biological lipids. Comparisons with the performance of conventional detergents suggests that the development of neutral or basic copolymers related to SMA could offer advantages, providing avenues for solubilization and analysis of a broader array of biological membrane:protein assemblies (memteins). The individual components of erythrocyte membranes including Rh proteins are well known, but their multimeric lipid complexes are dissociated in detergent-based preparations and hence no longer recognizable or extractable using conformation-specific antibodies. A set of ABCG2 protein constructs were designed with N-terminal GFP or SNAP and His 6 tags and solubilized from HEK cells using SMA(2:1) copolymer, as were CD28 and CD86 Antibiotics include lipid-specific peptides that self-associate into pores, which permeabilize bacterial membranes.	./cache/cord-299270-fwbz3t25.txt	./txt/cord-299270-fwbz3t25.txt