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Membrane microstructural templates for enzyme domain formation
Author(s) -
Maloney K. M.,
Grandbois M.,
Salesse C,,
Grainger D. W.,
Reichert A.
Publication year - 1996
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/(sici)1099-1352(199634/12)9:5/6<368::aid-jmr267>3.0.co;2-s
Subject(s) - template , enzyme , domain (mathematical analysis) , chemistry , membrane , nanotechnology , materials science , biochemistry , mathematical analysis , mathematics
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 A 2 , 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.