Heat-modifiable outer membrane proteins of Neisseria meningitidis and their organization within the membrane.
Neisseria meningitidis group B serotype 2 strain M986 contains two predominant outer membrane proteins, with apparent molecular weights of 41,000 (protein b) and 28,000 (protein e). Heating of outer membrane vesicles at 56 degrees C for 20 min caused much of b** to disaggregate and denature into b (41,000 daltons). In contrast, protein e could be rapidly solubilized by SDS at room temperature into its monomeric state (e*), but it was not converted to its final higher apparent molecular weight of 28,000 (e) unless heated at 100 degrees C for 2 min. We propose that protein b exists in the membrane as trimers or tetramers in a transmembrane configuration and that protein e exists as subunits on the exterior surface of the outer membrane and has a highly ordered tertiary structure.
D001426:Bacterial Proteins; D002462:Cell Membrane / Q000032:analysis; D006358:Hot Temperature; D008565:Membrane Proteins; D008970:Molecular Weight; D009345:Neisseria meningitidis / Q000032:analysis* / Q000648:ultrastructure; D011487:Protein Conformation; D011489:Protein Denaturation
D001426:Bacterial Proteins; D008565:Membrane Proteins