Globular proteins are usually water soluble, they are hydrophilic on the outside and they are

hydrophobic on the core so their structure is driven by three dimensional tertiary and quaternary
structures is driven by the hydrophobic effect. Globular structure

Fibrous proteins are insoluble fibers, not soluble in water and examples are collagen and keratin. It is a
long structure

General themes of fibrous proteins

1. Contain a single, repeating secondary structure

- They are either all or some helical or beta sheet
- In collagen and keratin, completely helical
2. They are hydrophobic
- Means they are made of most of nonpolar amino acids
- What happens when you spill water on your finger nails? Finger nails are made up of keratin and
keratin is water soluble so it would just completely dissolve
3. Polymeric chain
- they are all polymers of protein that pack together to form supra (big) molecular structures

Collagen

- Most plentiful protein in the body

- ¼
- Present in connective tissue, tendons, blood vessels and cornea
- Function is to be strong enough to hold teeth in the gums, eyeballs in the head
- Supra molecular structure
- Exists outside of the cell

Why is collagen so strong? All starts with the primary sequence. Each strand is made of the basic
repeating primary structure. Has a glycine every third residue from n to c.

X,y: proline, hydroxyl proline, hydroxy lysine or alanine

Collegen is a triple helix so each strand is its own helix and they wound together to form a bigger helix

Proline add a kink in the backbone and has hydrophobic side chain, a sharp turn that it turns every third
residue

Hydroxyproline also adds a kink, hydrophobic, being able to have hydrogen bonding which would
increase the strength of the structure

The small side chains alleviate the torsional stress along the backbone (glycine and alanine- nonpolar)

Hydroxyl lysine allows for covalent cross linking between triple helix that forms the supra molecular
structure