Unit One Grade 12 Biology Study Notes

Topics: Protein, Amino acid, Enzyme Pages: 7 (1316 words) Published: October 14, 2013
Macro molecules

Lipids (Fats, phospholipids, sterols)

Fats
used to insulate the body as well as protect organs

SATURATED
-better for you
-one or more double bonds between carbons
-less hydrogens
-oils (sunflower, flax)
-lower melting point

UNSATURATED
-worse for you
-single bonds between carbons
-more hydrogens
-animal fats
-higher melting points

Phospholipid
-2 fatty acids, 1 glycerol, - phosphate group, + choline group -hydrophobic tails
-hydrophilic heads

Phospholipid Bilayer
Groupings of phospholipids move together and create a protective membrane with the hydrophilic heads one the outside and very inside of the cell and the hydrophobic tails facing one another.

Sterols
-4 hydrocarbon chains fused together
-many functional groups attached
CHOLESTEROL
-a big part of the cell membrane
- cells turn cholesterol into vitamin D and bile salts

Carbohydrates (mono, di, poly saccharides)

Monosaccharides- hold energy and store it for cellular respiration Simple sugars – provide short term energy and storage
-most common one is Glucose (C6H12O)
-glactose and fructose are chemical isomers meaning they have the same chemical formula but different structures.

Disaccharides
2 monosaccharides combined
glucose + glucose = maltose

Polysaccharides
Many monosaccharides combined together to create STARCH, CELLULOSE and GLYCOGEN

Starch (amylose-simpler diagram)- long term energy and storage Glycogen (more branched diagram) - unused glucose is turned into glycogen and stored for later use

Cellulose- plant cells are made of this which is why they are rigid. Used in digestion in humans, cleans out colon and intestines.

Proteins – building blocks of life

Amino acids – organic compound containing an amino and a carboxyl group Have R-groups or side chains that are responsible for how it bonds with other amino acids. The bonds between amino acids are peptide bonds. NON POLAR LIKES NON POLAR

POLAR LIKES POLAR
POSITIVE LIKES NEGATIVE

Primary structure
A bunch of amino acids bind together through a certain sequence coded in the DNA -the number and order of acids is specific to each different protein

Secondary Structure
Peptide chains begin to bond with each other through the r groups. Bonds done in the secondary structure are usually done between amino acids close together. This causes the polypeptide chain to become ALPHA HELIX or a BETA PLEATED SHEET

-main bonds are hydrogen bonds between the carboxyl and oxygen atoms

Tertiary Structure
More bonds occur between amino acids but this time they are father apart from each other causing it to bend and fold even more

4 bonds
DISULPHIDE BOND- a bond between cysteine amino acids
ELECTROSTATIC BOND- an ionic bond between negative a positive side chains HYDROGEN BONDS- a bond between polar r-groups
HYDROPHOBIC INTERACTIONS- a bond between non-polar r-groups

Quatrinary Structure
Highest level of organization
The bonding of two or more tertiary proteins, making a lot of proteins into functional proteins.

Dehydration synthesis- removal of h2o and putting two molecules together Hydrolasis- adding of water and breaking apart two molecules Redox- give an electron away = oxidized, getting an electron = reduced

Homeostasis
The constant state cells try to be
Certain things pass in and out of the cell at specific times and rates so that the internal environment stays stable. Concentration gradient- difference between and are of high and an area of low concentration Brownian motion- the continuous movement and collision between molecules in a liquid

Passive transport – needs no energy
Simple diffusion- the movement of molecules from an area of high to low concentration. Small uncharged molecules like oxygen are passed through the membrane of a cell easily so that the cell can have oxygen.

Osmosis- movement of water across a semi permeable membrane from and area...
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