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The internal cavity of the staphylococcal alpha-hemolysin pore accommodates approximately 175 exogenous amino acid residues.

Abstract:

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 inserted at a position located within the cavity of the fully assembled heptameric alp...

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Publication status:
Published

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Publisher copy:
10.1021/bi0473713

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Journal:
Biochemistry
Volume:
44
Issue:
25
Pages:
8919-8929
Publication date:
2005-06-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:d36210e5-190f-4341-8c0d-47afae8407a4
Source identifiers:
52229
Local pid:
pubs:52229

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