English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Isolated purified contractile tail sheaths of bacteriophage T2L were analyzed for their carboxyl terminal amino acids by carboxypeptidase treatment and hydrazinolysis. Glycine and serine were identified as the only two carboxyl end groups. Using corrections for the yields of these two amino acids upon hydrazinolysis, we calculated that there are 154 (+/-30) moles of C-terminal glycine and 130 (+/-45) moles of C-terminal serine per mole of sheath. It appears likely that sheaths contain two types of polypeptide chains in equal numbers, probably 144 of each. The relation of these two components to the mechanism of sheath contraction is discussed.

Number of Polypeptide Components in Bacteriophage T2L Contractile Sheaths