PROTEINS, CARBOHYDRATES, LIPIDS, NUCLEIC ACIDS TEST REVIEW Flashcards
Life on earth is ___
Carbon based
Organic chemistry is the study of __
Carbon compounds
Why is carbon important in biochemistry
Carbon has 4 available covalent bonds which allow other atoms to bond to. Has the ability to form straight bonds with different types of elements allowing it to have a huge variety of complex molecules
Examples of carbon bonded molecules (4)
Polypeptide, glucose, lipids, triglyceride (neutral fat)
What is a polymer
large molecule formed from larger subunits of smaller molecules
Examples of polymers
DNA, Starch, Protein
What’s another name for polymerization
Dehydration synthesis
How does dehydration synthesis work
Monomers become a polymer and water is produced
What’s the opposite of dehydration synthesis
Hydrolysis
How does hydrolysis work
Uses water to break apart polymers into monomers. its the opposite of dehydration synthesis
What does the process of hydrolysis usually use and what’s it called
Enzymes called hydrolytic enzymes
Monomer
molecule that can be bonded to other identical molecules to create a polymer
Polymer
Multiple
What elements are proteins composed of?
C, H, O, sometimes N, S
What are ALL proteins composed of and how are they linked together?
They are composed of amino acids and linked by dehydration synthesis.
How many types of amino acids are there?
20
Examples of structural proteins and its function (3)
Keratin (hair, nails), collagen and elastin (skin)
Examples of proteins used for muscle function (2)
Actin and Myosin used for movement
Examples of enzymes and its function (3)
Lactase, sucrase, maltase. Used to speed up chemical reactions. Most enzymes end with “Ace”.
Examples of protein hormones and its function (3)
- Insulin used to lower blood sugar.
- Glucagon used to raise blood sugar.
- There are also growth hormones. Individuals that lack this suffer from dwarfism.
Example of blood protein and its function
Hemoglobin. It is found in red blood cells and are used to carry O2, CO2, and H+ ions.
Example of Immunoglobin
Antibodies. Used to attach specific virus receptor to prevent virus from replicating.
Examples of plasma protein (2)
Fibrinogen and Prothrombin. They are used in blood clotting. All plasma protein is made in the liver.
Where are carrier/channel proteins found and what are the functions?
They are found in cells. Its purpose is to transport molecules in and out of the cell
What is microfilament/microtubules and its function?
They form the cytoskeleton of a cell. It keeps the cell structure from collapsing.
What do R groups do to an amino acid?
R groups (remainder) determines the type of amino acid it becomes
What is the word used to link amino acids to create a chain?
Polymerization and dehydration synthesis
What is the bond that connects the amino acids called?
Peptide bonds
1 amino acid is called
Amino acid
2 amino acid linked is called
Dipeptide
3 amino acid linked is called
Tripeptide
More than 5 amino acids linked is
Polypeptide
50-70 amino acids linked is called
Protein
Why do all proteins have different shapes?
They have different shapes because proteins have different functions
What does primary structure look like
Chain of amino acids
Examples of primary structure
Actin/myosin (muscles)
What are the bonds associated with primary structure
Peptide bonds
Cause of the shape on primary structure
Peptide bonds between amino acids
What does secondary structure look like
Twisting of helix
Examples of secondary structure
Elastin (skin)
What are the bonds associated with secondary structure
Hydrogen bonds
Cause of the shape on secondary structure
Occurs because of partially positive H and a partially negative O
What does tertiary structure look like
3D globular shape composed of 1 and 2 level structure of1 proteins
Examples of tertiary structure
Enzymes
What are the bonds associated with tertiary structure
Ionic, covalent, hydrogen, disulfide bonds
Cause of the shape on tertiary structure
R groups
What does the quartenary structure look like
More than one tertiary protein together into a globular mass
Examples of quartenary structure
Hemoglobin
What are the bonds associated with quartenary structure
Multiple. Ionic, hydrogen, covalent, sulfur, disulfide bonds
Cause of the shape on quartenary structure
Between R groups
What is denaturation in protein
Process where a protein’s shape is altered causing it to lose its function
3 methods of denaturation in protein, what bonds are affected and examples:
- Temperature, hydrogen bonds, egg whites solidifying in heat.
- Change in pH, hydrogen bonds, lemon juice (acidic), milk curdling.
- Heavy metal, ionic bond, mercury, lead (attaches to enzyme and loses shape)
3 methods of denaturation in protein, what bonds are affected and examples:
- Temperature, hydrogen bonds, egg whites solidifying in heat.
- Change in pH, hydrogen bonds, lemon juice (acidic), milk curdling.
- Heavy metal, ionic bond, mercury, lead (attaches to enzyme and loses shape)
What are the 3 types of carbohydrates
glucose, starch, cellulose
Elements found in carbohydrates
C, H, O
Empirical formula of all carbohydrates
CH2O
What is always the ratio of carbohydrates
2 Hydrogen and 1 Oxygen
4 functions of carbohydrates:
- SHORT TERM energy storage (glucose is converted to starch in plants and glycogen in animals)
- Structural support in plants (cellulose found in wall of plant cell)
- Identification markers on cell membrane
- Insulation
Name of one sugar
Monosaccharides
Name of 6 carbon sugar
Hexose
Empirical formula of glucose
C6H12O6
Name of two sugars linked together through dehydration synthesis
Disaccharide
Famous disaccharides (3):
- Glucose + glucose = maltose (beer, scotch)
- Glucose + fructose = sucrose (table sugar)
- Glucose + galactose = lactose (breast milk)
Many sugars linked together are referred to
Polysaccharides
Famous polysaccharides and what are they found in (3)
Starch (plants) , glycogen (animals) , cellulose (plants)
Unit molecule of for sugars
Glucose
Characteristics of cellulose (3):
- Found in plant cell walls
- Beta B bonding (undigestible)
- 3000 glucose unit with NO SIDE BRANCHES
Characteristics of starch (3):
- Energy storage in plants
- Alpha bonding (digestible)
- 1000 glucose molecules with LITTLE SIDE BRANCHES
Characteristics of glycogen (3):
- Energy storage in humans
- Alpha bonding (digestible)
- 16-24 glucose unit with MANY SIDE BRANCHES