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. 1983 Feb;153(2):950–954. doi: 10.1128/jb.153.2.950-954.1983

N-terminal amino acid sequencing of EDP208 conjugative pili.

L S Frost, G D Armstrong, B B Finlay, B F Edwards, W Paranchych
PMCID: PMC221718  PMID: 6130062

Abstract

EDP208 conjugative pili contain a single polypeptide subunit of 11,500 daltons with a blocked N-terminus. This N-terminal blocking moiety was identified as an N-acetyl group by 1H nuclear magnetic resonance analysis of an N-terminal tripeptide isolated from pronase digests of EDP208 pilin. Limited acid hydrolysis of the tripeptide allowed its sequence to be determined as acetyl-NH-Thr-Asp-Leu. Trypsin digestion of EDP208 pilin resulted in the quantitative release of a fragment containing 12 residues from the N-terminus of the protein. The sequence of this dodecapeptide was determined to be acetyl-NH-Thr-Asp-Leu-Leu-Ala-Gly-Gly-Lys-Asp-Val-Asp-Lys.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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