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Amino acids link to one another by peptide bonds which form through a dehydration reaction that joins the carboxyl group of one amino acid to the amine group of the next in a head-to-tail manner to form a polypeptide chain. The chain has two ends – an amine group, the N-terminus, and an unbound carboxyl group, the C-terminus. [2]
The lipid-anchored protein can be located on either side of the cell membrane. Thus, the lipid serves to anchor the protein to the cell membrane. [1] [2] They are a type of proteolipids. The lipid groups play a role in protein interaction and can contribute to the function of the protein to which it is attached. [2]
Peptides are short chains of amino acids linked by peptide bonds. [1] [2] A polypeptide is a longer, continuous, unbranched peptide chain. [3] Polypeptides that have a molecular mass of 10,000 Da or more are called proteins. [4] Chains of fewer than twenty amino acids are called oligopeptides, and include dipeptides, tripeptides, and tetrapeptides.
Polyglutamic acid (PGA) is a polymer of the amino acid glutamic acid (GA). Depending on where the individual monomers connect, PGA can be gamma PGA (poly-γ-glutamic acid, γ-PGA), the form where the peptide bonds are between the amino group of GA and the carboxyl group at the end of the GA side chain, or alpha PGA, the form where the alpha-carboxyl is used to form the peptide bond.
Proteases, which are themselves proteins, come in several types according to the particular peptide bonds that they cleave as well as their tendency to cleave peptide bonds at the terminus of a protein (exopeptidases) vs peptide bonds at the interior of the protein (endopeptidases). [107] Pepsin is an endopeptidase in the stomach.
Lectins have a role in recognition at the cellular and molecular level and play numerous roles in biological recognition phenomena involving cells, carbohydrates, and proteins. [1] [2] Lectins also mediate attachment and binding of bacteria, viruses, and fungi to their intended targets. Lectins are found in many foods.
A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide. This is in contrast to an aminopeptidases, which cleave peptide bonds at the N-terminus of proteins. Humans, animals, bacteria and plants contain several types of ...
Glycolipid. Glycolipids are lipids with a carbohydrate attached by a glycosidic (covalent) bond. [1] Their role is to maintain the stability of the cell membrane and to facilitate cellular recognition, which is crucial to the immune response and in the connections that allow cells to connect to one another to form tissues. [2]