BIOMOLECULES (Lipids (Uses (Insulation, Long term energy, Cushions some…
Fats: very long chains
Long term energy
Cushions some organs
Helps form steroids/hormones
Structural component of cell membranes
Carries vitamins A,D,E,K
Made of 3 fatty acids & 1 glycerol
Single carbon bonds
Harder to break
Solid at room temperature
Too much can lead to heart disease
Double carbon bond
Easier to break
Liquid at room temperature
Steroids & Cholesterol
High density lipoprotein: Attaches to LDL and transports them away from the arteries.
Low density lipoprotein: Very large structure, attaches to artery walls and can build up enough to clog the artery.
Long chains of fatty acids (glycerol) joined to a carbon or alcohol molecule.
Insoluble in water
Comes from animal (beeswax, lanolin, spermaceti) and plants (cuticle, carnauba wax)
Forms structural components in all cells
Used to make enzymes & hormones
Made of long polymer chains of repeating amino acids
Made of 20 amino acids.
Different orders and numbers of amino acids will form different proteins.
There are 8 essential amino acids.
The human body can not make amino acids, they must be consumed.
The human body digests proteins and rearranges the sequence to make proteins that the body needs.
All bonds are covalent
Proteins have four levels of structure.
Primary: A sequence of a chain of amino acids. Unique and single strand of protein. Peptide bonds hold the polypeptide chain together.
Secondary: depending on the amino acids, the protein will fold or curl due due hydrogen bonds forming. Example: Myoglobin, hydrogen bonds hold alpha helices together.
Tertiary: Interactions between differentiators ("R" groups") occur. They either attract or repel. Hydrogen bonds, polar & non-polar, and disulfide bonds all have a part in determining the final shape of a tertiary protein.
Quaternary: Large globular proteins. They can have two or more proteins involved. Example: Hemoglobin attracts oxygen and makes oxyhemoglobin.
Denaturation & Coagulation
Heat can disrupt the hydrogen bonds and non-polar hydrophobic interactions in protein, causing them to become denatured.
If the pH is too low, it can change the charge of a protein, causing it to become a precipitate. If it is too high , it can change the charge causing the like charge to repel each other, possibly unfolding the protein.
Temporary change in configuration of the protein.
Permanent change in configuration of the protein.
RNA: Copies genetic information and transforms in into a protein that the body is able to read.
DNA: Holds genetic information.
The human body can not produce carbohydrates, it must consume them.
If carbohydrates are not used, they will be stored as fat.
It is the biggest form of energy in the human body.
Either single sugar unit or polymers of many sugar units.
Formula follows 1:2:1 ratio
Can be classified in three different groups
Made of one sugar unit
Glucose, galactose, fructose
These are isomers. They have the same chemical formula, but different structures.
Different chemical properties can be explained using the different chemical structures.
Hydrolysis breaks a disaccharide into two monosaccharides by adding water.
Dehydration synthesis joins two monosaccharides together, with a covalent bond, through the removal of water.
Three or more monosaccharides.
Stores energy (EX. Starch, Glycogen, and Cellulose.)
Starch is energy storage in plants. Glycogen is used to store energy in the human liver. Cellulose is found in cell walls of plants.
Energy is stored in its bonds, it is released when you form a bond.
A, B, C, D, E, K, Carotenoids
Required in small quantities to perform physiological functions.
Must be eaten, the body can not produce them.
Boron, Calcium, Cobalt, Fluoride, Iron, Lithium, Magnesium, Selenium, etc.
Help preserve and keep the body and brain working well.