These domains are located near the N-terminus of the protein.

It is a domain commonly found in the N-terminus of many proteins.

This acetyl group is added to the front end, or N-terminus of the new protein.

One of these lies towards the N-terminus of the protein.

Most of these proteins contain a short conserved region at their N-terminus.

The N-terminus can be modified by the addition of a myristoyl anchor.

It is fused to the N-terminus of a protein.

The N-terminus is also well structured with a turn resembling that of a classical beta-turn.

When the N-terminus dissociates it can be found in lipid rafts.

It is known that the N-terminus of the protein kinase binds on the cell wall.

The N-terminus of the protein has a region demonstrated to be able to bind microtubules.

Cobatoxin 1 has a rod-like shape due to an extended N-terminus.

One is at the N-terminus and is responsible for inhibiting angiogenesis.

These samples are used in the step-by-step identification by testing and coupling starting at the N-terminus.

Its signal peptide is at the N-terminus but is not cleaved off.

This domain occurs towards the N-terminus of the proteins in this entry.

The greatest differences occur near the N-terminus.

The putative 622-amino acid protein has a leucine-zipper motif at its N-terminus.

The catalytic domain of polo-like kinases is located in the N-terminus.

Both the C-terminus and the N-terminus face the cytoplasmic side of the membrane.

There are two isoforms of caveolin-1: caveolin-1α and caveolin-1β, the latter lacking a part of the N-terminus.

The two isoforms differ only in their N-terminus, which has been shown by one group to be important for membrane localization.

The N-terminus of the protein associates with β subunits.

Both isoforms shared 11 amino acids between signal sequences of the N-terminus.

The N-terminus is exposed to the solvent.