N terminus

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a·mi·no-ter·mi·nal

(ă-mē'nō-ter'min-ăl),
The α-NH2 group or the aminoacyl residue containing it at one end of a peptide or protein (usually on the left as written).
Synonym(s): NH2-terminal

N terminus

The front end of a polypeptide chain, which has a free (unattached) amine (NH2) group.

a·mi·no-ter·mi·nal

(ă-mē'nō-tĕr'mi-năl)
The α-NH2 group or the aminoacyl residue containing it at one end of a peptide or protein (usually at left as written).
References in periodicals archive ?
The peptides range from 2-14 amino acids in length where half of the unique sequences have a proline at the second position from the N-terminus, indicating a possible structural pattern for DPP-IV-inhibitory peptides.
CueO protein with a His-tag on its N-terminus was expressed in BL21 cells, transformed with Recombinant pET 28a vector and later grown in LB medium at 37AdegC after IPTG induction.
The plasmids used for knockdown of Nesprin-2 targeting the N-terminus and the C-terminus (Nesprin-2 N-term shRNA, Ne-2 N-term KD; Nesprin-2 C-term shRNA, Ne-2 C-term KD) as well as the control have been described previously [7].
Charge screening of the C-terminus either by Na or Ca ions and N-terminus by Cl ions, respectively, increases radiation adsorption of C=O and N-H, implying a molecular geometry more prone to H bond interactions that would be consistent with the larger size of the nanotubes in the presence of these salts.
Accordingly, we constructed our candidate adjuvant TCTA1T by fusing HIV-1 Tat PTD onto both N-terminus and C-terminus of CTA1 subunit, which consequently allowed bypassing of CTB-dependent cellular internalization of CTA1 (Figure 1(a)).
HSA has a high affinity metal binding site at the N-terminus.
However, we now know that albumin has two additional cobalt binding sites, which have a higher affinity than the N-terminus (i.e., site A and site B), as well as an additional fourth binding site (i.e., Cyt-34) [3-6].
Some authors reported DNA methylation followed by histone modifications, such as changes in lysine in the N-terminus of histones by histone acetyltransferases [4,5].
The rhEGF used in GeneSoft contains a patented extra three amino acids in the N-terminus, which confer original rhEGF with additional commercial benefits, including better stability.