ISSN:
0952-3499
Keywords:
proteins
;
lipid monolayers
;
interfacial recognition
;
membranes
;
domains
;
two-dimensional crystallization
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Medicine
Notes:
Soluble proteins can spontaneously self-organize into two-dimensional domains at membrane interfaces, given sufficient mobility and specificity to membrane-localized ligands. The authors' recent results studying interfacial domain formation of the membrane-active enzyme, phospholipase A2, indicate that latertal phase separation of heterogeneous membrane mixtures creates anionic templates of specific morphology onto which the enzyme deposits, forming large protein assemblies. Selective removal of membrane components (lysolipid or fatty acid) produces different enzyme interfacial responses and domain morphologies. This leads to the conclusion that complex chemical and physical interactions laterally in the lipid membrane interface as well as between bound protein molecules play a role in organizing protein structures.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
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