C terminus

(redirected from Carboxyl terminus)

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 ?
The product of TSC2 gene, tuberin, which consists of 1807 amino acids, is known to have seven domains including a leucine zipper region, two small coiled-coil domains (CCD1, CCD2), a small region of similarity with GTPase-activating protein (GAPD), two transcriptional activation domains (TAD1, TAD2), and a calmodulin-binding site (CaMD) in the carboxyl terminus of tuberin.
Virus genotyping was based on the 450-nt coding sequence for the carboxyl terminus of nucleoprotein (N) of measles virus, as recommended by the World Health Organization (3,6).
GRA8 contains an amino terminal signal peptide, three degenerate proline-rich repeats in the central region and a transmembrane domain near the carboxyl terminus (21).
NIS is a protein with 13 putative transmembrane domains, an extracellular amino terminus, and an intracellular carboxyl terminus (De La Vieja et al.
Identification of the low density lipoprotein receptor-binding site in apolipoprotein 13100 and the modulation of its binding activity by the carboxyl terminus in familial defective apo-13100.
Called CHIP (carboxyl terminus of Hsc70-interacting protein), this molecule decides the fate of malformed proteins in heart muscles, says Cam Patterson of the University of North Carolina at Chapel Hill.
The carboxyl terminus of the fatty acid is reactive and is the end of the molecule that binds the fatty acid to other molecules.
All the changes of the 532 amino acid (aa) N protein occurred at the carboxyl terminus, with the following mutations: I429V, G432E, N457D, 1502T, E511G, L518P, and A521T.
Lamins A and C are coded by a single developmentally regulated gene designated LMNA; lamin C is a splice variant and lacks the carboxyl terminus present in lamin A.
The biologically active portion of the molecule is its amidated carboxyl terminus. All forms of CCK larger than CCK-8 are biologically active.
The matrix accumulates the highest level of mutations in the entire open reading frame; by contrast, the N is modified in the carboxyl terminus, and the H has biased hypermutation in a limited region (5,6).
Evidence indicates that the arginyl residue at the carboxyl terminus is also removed.