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 ?
Truncation at the C-terminus causes a dramatic decrease in pore-forming activity toward erythrocytes but not toward liposome: The specific haemolytic activity, defined as the lowest concentration of the toxin causing 50 per cent haemolysis of a 1 per cent suspension of erythrocytes at 25[degrees]C in 1 h, of purified VCC toward rabbit, sheep and human erythrocytes was in the range of 100-400 picomolar.
Signature coding mutations that were observed in >3 viruses are summarized in Table 2, and the amino acid alignment of the deduced G protein C-terminus region from the unique nucleotide sequences among the combined Kenyan ON1 and GenBank collated dataset is shown in Figure 4.
Lpp truncations at 10-30 residues upstream of the C-terminus were also created to isolate the residues that are responsible for the binding of surface-exposed Lpp to plasminogen.
Based on recent submissions by Intellect, the USPTO allowed patent claims directed to treatment methods that use antibodies that recognize the free C-terminus of beta amyloid 1-40.
This method can directly measure circulating cTnI to determine if it is phosphorylated or degraded at either the N- or C-terminus.
Using peptides commercially available as both acid and amide forms at the C-terminus, fragmentation studies have been conducted using collision-induced dissociation (CID) and electron transfer dissociation (ETD) mass spectrometry methods with electrospray ionization/quadrupole ion trap (ESI/QIT).
All these complex receptors have an extracellular N-terminus and an intracellular C-terminus with the seven transmembrane-spanning domains making up the opioid binding pocket with distinct agonist and antagonist conformations.
a comovirus such as CPMV) having a beta-barrel structure at an immunogenically effective site, such as in a loop connecting beta sheets or at/near the C-terminus.
These longer beta-amyloid peptides have been notoriously difficult to make, due to a C-terminus sequence composed primarily of hydrophobic amino acids.
An [approximately equal to]2,100-nt fragment of the C-terminus of the rat HEV V-105, nt 4923-poly (A) tail, was amplified with a pair of primers, F13 and TX30SXN, by the first RT-PCR.