In 50 % of eukaryotic proteins the N-terminus is acetylated.

This modified amino acid is obtained when synthesizing peptides with C-terminal Cys.

backwards from the C-terminal end to the N ..

Figure 1. Schematic representation of the covalent structure of a protein, showing the N-terminus as the first residue in the polypeptide chain. The square brackets indicate the repeating part of the chain (the backbone), and the R group denotes the variable side chain of each amino acid residue. The C-terminus is the last residue in the chain.

Howard Dintzis showed in 1961 that synthesis was from N-terminus to C-terminus.

cytoplasm for the further use in protein synthesis.

The other approach is to introduce backbone protecting groups which will prevent the formation of hydrogen bonds. Such protection is made by the introduction of the Hmb group on the αnitrogen [53]. It has been shown that the presence of a Hmb unit every 6-7 residues is sufficient to disrupt the peptide aggregation [54]. The Hmb protected amino acid is introduced under the form of N,O-bis-Fmoc-N-(2hydroxy-4-methoxybenzyl) derivative, the O-Fmoc protection being cleaved during the following piperidine treatment. At the end of the synthesis the Hmb group is cleaved in the final TFA cleavage.

T1 - N-terminal-based targeted, inducible protein degradation in Escherichia coli

N2 - Ribosomal proteins are a major component of ribosomes, which catalyze protein synthesis. One ribosomal protein, L7a (RPL7a), which is a component of the 60S large ribosomal subunit, has additional functions involved in cell growth and differentiation that occur via interaction with human thyroid hormone receptor (THR) and retinoic acid receptor (RAR) and in turn inhibit the activities of the two nuclear hormone receptors. In this study, the N-terminal domain of human RPL7a was overexpressed in Escherichia coli using an engineered C - terminal His tag. The N-terminal domain of human RPL7a was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 3.5 Å from a crystal belonging to the tetragonal space group P4122 or P4322 with unit-cell parameters a = 92.28, b = 92.28, c = 236.59 Å.


Chemically synthesized peptides have free N-termini

Messenger RNA (mRNA), the blueprint for protein synthesis, is written in the language of ribonucleotides (A, G, C, U) and is read in blocks of three nucleotides that mean a particular amino acid or termination.

N-terminal to C-terminal direction

The base catalyzed elimination of the suffhydryl protecting group affords dehydroalanine and the subsequent addition of piperidine yields the C-terminally modified peptide [69]. This side reaction is minimized (but not avoided!) when trityl is used for the protection of the C-terminal Cys.

protein H contains four predicted C-terminal ..

Diketopiperazine formation may be circumvented in Fmoc/tBu SPPS

- by using 2-chlorotrityl chloride resin or other bulky resins such as DHPP-Resin.
- by coupling the appropriate Fmoc-dipeptide in lieu of the penultimate amino acid. In that case a risk of epimerization exists if the C-terminal amino acid of this dipeptide is not Gly or Pro.

Resins for the Synthesis of C-Terminal Modified ..

The extent of diketopiperazine formation depends on the nature of the C-terminus as well as on the penultimate amino acid, especially on the bulk of the side-chains.

to give access to peptides with diverse C-terminal ..

Good accessibility to the ester bond facilitates this side-reaction as does a cis-amide bond making sequences containing a C-terminal Pro prone to this side-reaction. Nearly quantitative loss may occur.