3.

PROTEINS
The

functional molecules

Ex. lactase, hemoglobin, hair keratin, insulin

a) Structural proteins Function: Support Example: Collagen and elastin provide a fibrous framework in animal connective tissues such as tendons and ligaments Keratin is the protein of hair, horns, quills,

Keratin

Collagen injection

b) Storage Proteins
Function: Storage of amino acids Ex. Ovalbumin is the protein of egg whites
Casein

is the protein is mammal milk

c) Transport Proteins
Function: transport other substances Ex. hemoglobin transports oxygen from the lungs to the other parts of the body

Other proteins transport molecules across cellular membranes

d) Hormones
Function: coordination of bodily activities Example: Insulin helps control the concentration of sugar in blood

Insulin

e) Receptor Proteins
Function: response of cell to chemical stimuli Ex. neuron receptors respond to chemicals released by other nerve cells

f) Contractile proteins Function: Movement Ex. Actin and myosin are the proteins responsible for muscle movement

g) Defensive Proteins Function: Protection against disease Ex. Antibodies combat bacteria and viruses

The Immune System

h) Enzymes Function: Speed up chemical reactions Ex. amylase hydrolyzes sugar polymers in food.

 Proteins

acids"

are "unbranched polymers of amino

 Amino

acids: small molecules containing a central C atom and a side chain

There are 20 amino acids in human food 8 of those are essential: we do not produce them and therefore must EAT them

protein is a linear chain of amino acids 20 species of amino acid, properties dictated by side chain (R) Polar (hydrophillic): contain O and N Nonpolar (hydrophobic) Acidic: negative charge H Basic: positive charge
NH3+ C R COO-

 Amino

acids link together during protein synthesis through peptide bonds to form a POLYPEPTIDE
Most functional proteins will contain hunderds and thousands of amino acids linked together

Peptide linkage

 As

the polypeptide lengthens it can fold into sheets (b-sheets) or wrap into coils (a-coils)

 Protein

function depends on its 3dimensional shape

Sickle Cell

Figure 3.9 Life 8e: Quaternary Structure of a Protein Hemoglobin consists of four folded polypeptide subunits that assemble themselves into the quaternary structure shown here. In these two graphic representations, each type of subunit is a different color. The heme groups contain iron and are the oxygen-carrying sites.

How Complex are Proteins?

Example: Average E. Coli protein: 300 a.a. long 20 possible a.a. at each position 20300 possible sequences (bigger than the number of atoms in the entire universe!)

DNA: structure is independent of sequence Protein: structure change with sequence change

 Both

shape and chemistry allow a protein to behave in a specific way

 Denaturation:

A denatured protein cannot carry out its original function

positives - fever: can denature bacteria - straightening/ curling hair - cooking meat negatives - fever: can cause damage - if peptide bonds are broken protein will be destroyed

a change in the three-dimensional shape of a protein caused by high temperatures or harsh chemical conditions (ex. acids, bases, salts)

Homework
1. Describe some groups of lipids that are not triglycerides. 2. What are the structural components of triglycerides?
3. How do saturated fats differ from unsaturated fats? 4. How can only 20 amino acids account for the many different proteins? 5. Define protein denaturation. Why is it important?