scholarly journals Receptor for bacteriophage lambda of Escherichia coli forms larger pores in black lipid membranes than the matrix protein (porin).

1979 ◽  
Vol 138 (1) ◽  
pp. 33-39 ◽  
Author(s):  
B A Boehler-Kohler ◽  
W Boos ◽  
R Dieterle ◽  
R Benz
2009 ◽  
Vol 162 (1-2) ◽  
pp. 179-183 ◽  
Author(s):  
Senthil Kumar Subramanian ◽  
Beng Ti Tey ◽  
Muhajir Hamid ◽  
Wen Siang Tan

1977 ◽  
Vol 72 (2) ◽  
pp. 292-301 ◽  
Author(s):  
A C Steven ◽  
B Heggeler ◽  
R Müller ◽  
J Kistler ◽  
J P Rosenbusch

Matrix protein (36,500 daltons), one of the major polypeptides of the Escherichia coli cell envelope, is arranged in a periodic monolayer which covers the outer surface of the peptidoglycan. Although its association with the peptidoglycan layer is probably tight, the periodic structure of the peptidoglycan. Although its association with the peptidoglycan later is probably tight, the periodic structure is maintained in the absence of peptidoglycan, and is therefore based on strong protein-protein interactions. A detailed analysis of the ultrastructure of the matrix protein array by electron microscopy and image processing of specimens prepared by negative staining or by freeze-drying and shadowing shows that the molecules are arranged according to three fold symmetry on a hexagonal lattice whose repeat is 7.7 nm. The most pronounced feature of the unit cell, which probably contains three molecules of matrix protein, is a triplet of indentations, each approx. 2 nm in diameter, with a center-to-center spacing of 3nm. They are readily penetrated by stain and may represent channels which span the protein monolayer.


Author(s):  
H.M. Mazzone ◽  
W.F. Engler ◽  
R. Zerillo ◽  
G.F. Bahr

The nucleopolyhedrosis virus (NPV) of the forest tent cater - pillar (Malacosoma disstria Hubner) has been analyzed in our laboratories. As a representative of the Baculovirus class, the NPV has virus particles enclosed with in a proteinaceous structure, the inclusion body.


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