Article
The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.
Biochemistry - 28 Jun 2005
Jung Yuni, Cheley Stephen, Braha Orit, Bayley Hagan
Abstract excerpt
The cavity within the cap domain of the transmembrane staphylococcal alpha-hemolysin (alphaHL) pore is roughly a sphere of diameter approximately 45 A (molecular surface volume approximately 39,500 A(3)). We tested the ability of the cavity to accommodate exogenous polypeptide chains. Concatemerized Gly/Ser-containing sequences ("loops", L; number of repeats = n; number of residues = 10n + 5, n = 0-21) were...
Topics
- Amino Acids
- Bacterial Toxins
- Base Sequence
- DNA, Bacterial
- Glycine
- Hemolysin Proteins
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Protein Denaturation
- Protein Structure, Tertiary
- Protein Subunits
- Serine
- Staphylococcus
- Temperature