C terminus

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C ter·mi·nus

the end of a peptide or protein having a free carboxyl (-COOH) group.

C terminus

The end of a polypeptide chain, which has a free (unattached) carboxyl (COOH) group.

C ter·mi·nus

(tĕr'mi-nŭs)
The end of a peptide or protein having a free carboxyl (-COOH) group.
References in periodicals archive ?
PSK precursor polypeptides share a conserved domain close to the C-terminus, from which mature functional PSK peptides are generated (Fig.
Since the C-terminus of NuMA1 containing the nuclear localization signals (NLSs), we deduced that products encoded by the short isoform would mainly exist in the cytoplasm region, instead of the nuclear region or spindle poles.
Somehow expectedly, our results indicate that phosphorylation of Claudin-3 Y-1 might abrogate the binding of the C-terminus of Claudin-3 towards the nNOS PDZ domain.
This construct has an Xpress tag at N-terminus and DsRed2 at C-terminus (Figure 1B).
All cholesterol binding toxins (CBT's) shows similarity in their primary amino acid sequence and identity in the so called undecapeptide region having tryptophan-rich loop that contains 11 amino acids, which is nearest to the C-terminus of the polypeptide chain [17].
Three distinct PSSs have been characterized in fish: PSS-I which contains SS-14 at its C-terminus, PSS-II which contains [Tyr7, Gly10]-SS-14 at its C-terminus, and PSS-III which contains [Pro2]-SS-14 at its C-terminus (Tostivint et al.
One of these antibodies is always specific for the intact cysteine ring, which is thought to be the active form, while the other antibody recognizes either the C-terminus of the peptide (Abbott AxSYM and Architect, Shionogi IRMA) or for the N-terminus (Alere Triage and Beckman Access).
To confirm the stable transfection of HEK293 cells a rabbit antibody against the C-terminus of the [[beta].
It was found that the di-leucine based motif was required for the full activity of MARCH1 and that the last 50 residues in the C-terminus were required for function possibly for substrate interaction or recruitment of downstream effectors leading to modulation of targets [58].
The C-terminus of KatG protein has enzymatic function, (19,20) and the truncated mutation lacking the C-terminal 41 amino acids is inactivate.
The functions of this surface-exposed Lpp have not been determined; however, the C-terminus is lysine rich, and other bacterial proteins with C-terminal lysines have been shown to bind plasminogen (2).
Antibody fragments fused at the C-terminus, N-terminus or bivalent forms as well as fusions to small or large peptides were compared to unfused albumin variants for FcRn affinity by SPR using Biocoree technology (Figure 2).