Notes

Proteins: Macromolecules composed of Amino Acids.
Amino Acids: A central carbon atom bonded with a hydrogen atom & 3 groups, Amino, Acidic, & the R Group, the remainder of the macromolecule.
Amino acids differ from these R Groups, which vary in structure.
Proteins are just large polypeptides
When 2 Amino Acids join a dipeptide the result, while a polypeptide has 3 or more Amino Acids., and there are 20 different Amino Acids that compose all polypeptides, this sequence is a “Primary Structure.”
The bond between Amino Acids is a Peptide Bond, which is when atoms share electrons unevenly, making hydrogen bonding possible in polypeptides, making it polar.
Hydrogen Bonding often twists these Polypeptides into coils, which creates the “Secondary Structure.”
Hydrogen, Ionic, & Covalent bonding occurs in Polypeptides, creating the Teritary Structure.
Hydrophobic portions occur inside the molecule while Hydrophillic is on the outside.
Some proteins only have 1 polypeptides while others have more, each has its own Teritary Structure.
If a protein has more than 1 polypeptide it’s given a Quaternary Structure.
When proteins are exposed to extremes in heat & PH they have an irreversible change in shape, this is called Denaturation & occurs when normal bonding of R Groups are disturbed.
1 protein loses its shape, and therefore no longer works well.
The alteration of protein organizations may hypothetically cure Alzheimer’s & Creutzfeld-Jacob Disease.
Metabolism is the result of chemical reactions that occur in a cell, most of these can’t happen unless an enzyme is present.
Enzymes are molecules that allow particular metabolic reaction to body temp.
Atoms & molecules frequently do not react unless they are activated.
Enzymes lower the energy of activation by forming a complex with particular molecules, bringing together atoms or molecules & cause reactions.
Our bodies convert sugar to CO2 & water & can do so at body temp.