Abstract:
:Atomic force microscopy has been used to study self-assembled structures of two alpha-hemolysin mutants. For a mutant (alphaHL-H5) that was locked into the prepore state on fluid phase egg-PC membranes, we visualized, for the first time, heptameric prepores and showed that the 7-fold axis in the prepore lies perpendicular to the membrane surface. For another mutant (TCM) with the transmembrane domain, the self-assembled oligomer that assumes the conformation of the fully assembled pore is also a heptamer. These results show that heptamers are the preferred oligomerization state of alpha-hemolysin.
journal_name
Microsc Res Techjournal_title
Microscopy research and techniqueauthors
Malghani MS,Fang Y,Cheley S,Bayley H,Yang Jdoi
10.1002/(SICI)1097-0029(19990301)44:5<353::AID-JEMkeywords:
subject
Has Abstractpub_date
1999-03-01 00:00:00pages
353-6issue
5eissn
1059-910Xissn
1097-0029pii
10.1002/(SICI)1097-0029(19990301)44:5<353::AID-JEMjournal_volume
44pub_type
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