Biological Molecule (Protein)

Structure

Functional Group

Hydroxyl grp., carboxyl grp., amine grp.

Shape

Quaternary structure, consists of 2 polypeptide chains of beta helix and 2 alpha helix in a globular shape subunits

Monomer

Myoglobin is the monomer of hemoglobin, made up of histidine aa.

Linkage

Intermolecular forces of attraction such as hydrogen bonding, van der Waals forces (attraction and repulsions between atoms), and dipole-dipole interactions. As well as covalent bonding

Types

Hemoglobin (Transport protein)

Collagen (Structural protein)

Functions

Hemoglobin

Hemoglobin is used for transferring oxygen in your blood from the lungs to the tissues. It binds oxygen to the heme group in globin and carries it from the lungs to all tissues and organs, and receives carbon dioxide from the tissues and organs and sends it back to the lungs

Collagen

Structural proteins strengthen cells, tissues, organs, etc. giving support and shape to organisms. Provides bone, tendons and ligaments with tensile strength, connective tissue and skin with elasticity

Structure

Functional Group

Hydroxyl grp., carboxyl grp., amine grp.

Shape

Quaternary structure, triple alpha (α) helix chains

Monomer

Amino acids consisting of glycine, proline and a modified version of proline, hydroxyproline

Linkage

Monomers are held by peptide bonds, helix chains are held together by hydrogen bonds, linking the peptide bond NH of a glycine with a peptide carbonyl (C═O) group hold the three chains together

Properties

- Non polar enabling collagen to be able to form strong hydrogen bonds - Hydrophobic - Insoluble in water