Wash the surface afterward to remove the remaining acid residue.

The new bonds form between amino acid residues at a different place from their original site.

They have sugar chains added to some of their amino acid residues.

There is a signal sequence of 19 amino acid residues.

The domain is about 90 amino acid residues long.

The consensus sequence is based on a 100% conservation of the three leading amino acid residues.

The amino acid residues are always joined by peptide bonds.

These donor groups are often provided by side-chains on the amino acid residues.

Each lobe is then divided into two domains of 160 amino acid residues.

The region consists of approximately 183 amino acid residues.

The amino acid residues at the contact interface differ with respect to their position and location in the 3-D structure.

The subscript indicates the number of amino acid residues in the fragment.

Each different protein has a unique sequence of amino acid residues: this is its primary structure.

It is a single polypetide chain consisting of 245 amino acid residues.

The 105 amino acid residue human precortistatin in turn is cleaved into cortistatin-17 and cortistatin-29.

The protein has 449 amino acid residues and localises to the nucleus.

They share a common conserved module of approximately 230 amino acid residues.

The leader sequence consists of the 22 N-terminal amino acid residues.

Modification of basic amino acid residues in the peptide chain.

The largest Rel protein, it consists of nearly 1,500 amino acid residues.

These inhibitors modify key amino acid residues needed for enzymatic activity.

Even larger cathelicidin peptides (39-80 amino acid residues) are also present.

There are different hydrophobicity scales of amino acid residues.

It encodes a protein of 377 amino acid residues.

This secreted polypeptide is between 78 and 80 amino acid residues in length.