β-barrel membrane proteins

Current Opinion in Structural Biology

Volumn 10, Issue 4, 2000, Pages 443-447

  Schulz, Georg E ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE ENZYME; MEMBRANE PROTEIN; MONOMER; OLIGOMER; OUTER MEMBRANE PROTEIN;

BETA CHAIN; CHLOROPLAST; CRYSTALLIZATION; GENETIC ENGINEERING; HUMAN; MITOCHONDRIAL MEMBRANE; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 0033932639     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(00)00120-2     Document Type: Review

References (47)

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40. 171 were deleted by short cuts in all possible combinations. The 16 resulting deletion mutants lost their biological functions in bacterial F conjugation and as bacteriophage receptors, but kept the membrane-embedded β barrel, as demonstrated by their resistance to proteolysis and thermal denaturation. The results confirm that the large external loops do not contribute to β barrel folding and stability.
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