BIOLOGY FINALS REVIEWER

CARBOHYDRATES
● Associated with sugar, energy, and starch

● Effective energy-yielding nutrients and building materials.

● By-product of photosynthesis
● Among the most abundant biological molecules in the World

● General formula: Cn(H2O)n

● Are composed of carbon, hydrogen, and oxygen (1:2:1 ratio)
● Carbohydrates mean “carbon plus water”.

● Unused carbohydrate is stored in the liver and muscles

● excess carbohydrate (when full) is stored as fat
● too little carbs will cause weakness, poor concentration, constipation

3 Types of Carbohydrates
❖ Monosaccharides
● Simplest form of sugar
● Basic unit
❖ Disaccharides
➢ Two monosaccharides joined together
❖ Polysaccharides
➢ Made up of repeating units of sugar joined together by glycosidic bonds.

Monosaccharides
● Mono means single.
● Saccar means sugar.
● ose - the suffix of most of the monosaccharides.
● Consist of one sugar unit.
● Chemical formula: C6H12O6

● Classification of monosaccharide based on functional group:

○ Aldose- If the sugar has an aldehyde group (R-CHO)
○ Ketose- If the sugar has a ketone group RC(=O)R')

● Classification of monosaccharide based on the number of carbons:

○ Triose- 3 Carbons (Glyceraldehyde)
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○ Tetrose- 4 Carbons (Erythrose)
○ Pentose- 5 Carbons (Ribose)
○ Hexose- 6 Carbons (Galactose)
ISOMER
● same chemical formula but differ structurally and chemically due to arrangement of
functional groups.

Example: Glucose, Fructose, and Galactose

● Glucose (C6H12O6)
○ Dextrose, blood sugar, or grape sugar.
○ to provide energy.
○ No digestion required.
○ Most abundant carbohydrate in the blood.
○ Glycosuria- glucose present in the urine.

● Fructose (C6H12O6)
○ Levulose
○ sweetest among the sugar.
○ found in fruits, honey, and corn syrups.
○ can be metabolized directly or converted to glucose in the liver

● Galactose
○ Aldohexose, brain sugar
○ Obtained from milk.
○ Serve as a blood marker.
○ Half as sweet as glucose.
○ Galactosemia- genetic metabolic disorder (usually infant) that affects how
the body processes galactose.

● Glyceraldehyde
○ simplest monosaccharide
○ Triose
● Erythrose
○ Pentose phosphate pathway
○ Erythrose
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● Ribose
○ Part of DNA and RNA (nucleic acids)
○ Pentose

Disaccharides
● Di means double.
● Two monosaccharides are joined together.
● Chemical formula: C12H22O11
● Glycosidic bond- the bond that joins the two simple sugars.
● Should be broken down to serve as fuel for cellular activities.

● Sucrose (G+F)
○ Table sugar
○ A combination of glucose and fructose (50:50).
○ Excellent natural preservative.
● Lactose (G+GL)
○ Found in milk.
○ Combination of glucose and galactose.
○ Lactase is needed to break this sugar.
○ Lactose intolerance- digestive disorder where the body cannot fully digest
lactose.
● Maltose( G+G)
○ Found in beer.
○ Composed of two glucose.
○ Provide energy in germinating seeds.

Polysaccharide
● Poly means many.
● Saccar means sugar.
● Made up of repeating units of sugar joined together by glycosidic bonds.

● Structural Polysaccharide- components of structural parts of living things such as

the cell wall of plants and animals.
○ Cellulose
■ most abundant organic molecule on earth.
■ support to cell walls of plants and bacteria.
■ Keeps our digestive tract healthy but not serve as nutrient
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○ Chitin
■ Principal component of exoskeletons of animals (mollusk and
crustaceans)
■ Used in making surgical threads, binders in dyes, fabrics, and
adhesives.

● Storage Polysaccharide- serves as storage of energy.

○ Starch
■ Derived from potatoes, wheat, bread, pasta, and other bread
products.
■ Hydrolysis is the major chemical reaction in the digestion of starchy
foods.
■ Ptyalin or salivary amylase- an enzyme that changes starch into
sugar.
○ Glycogen
■ Animal starch is stored in liver and muscle.
■ From excess glucose in the body.

Glycogen to Glucose (break down)- Glycogenolysis

Glucose to Energy (break down)- Glycolysis
Glucose to Glycogen (break up)- Glycogenesis

● Oxygen ( O8) 16.0

○ Atomic mass: 16.0
○ % of human weight: 65%
○ Function in life: part of water
and most organic molecules.
● Carbon (C6)
○ Atomic mass: 12.0
○ % of human weight: 18%
○ Function in life: the
backbone of all organic
molecules.
● Hydrogen (H1)
○ Atomic mass: 1.0
○ % of human weight: 10%
○ Function in life: part of all
organic molecules and of
water.
● Nitrogen (N7)
○ Atomic mass: 14.0
○ % of human weight: 3%
○ Function in life: components
of proteins and nucleic acids
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● Calcium (Ca 20)
○ Atomic mass: 40.1
○ % of human weight: 2%
○ Function in life: constituent of
bone.
○ Essential for the action of
nerves and muscle.
● Phosphorus (P15)
○ Atomic mass: 31.0
○ % of human weight: 1%
○ Function in life: part of cell
membrane and of energy
storage molecules.
○ a constituent of bone.
● Potassium (K19)
○ Atomic mass: 39.1
○ % of human weight: 0.3%
○ Function in life: Important in
nerve action.
● Sulfur (S16)
○ Atomic mass: 32.1
○ % of human weight: 0.2%
○ Function in life: structural
component of most proteins.
Organic Molecules
● Oxygen- part of most organic molecules and of water.
● Carbon- backbone of all organic molecules
● Hydrogen- part of all organic molecules and of water.
● Sodium (Na 11)
○ Atomic mass: 23.0
○ % of human weight: 0.1%
○ Function in life: the primary
ion in body fluids
○ important for nerve action.
● Chlorine (Cl 17)
○ Atomic mass: 35.5
○ % of human weight: 0.1%
○ Function in life: component of
digestive acid
○ A major ion in body fluids.
● Magnesium (Mg 12)
○ Atomic mass: 24.3
○ % of human weight: Trace
○ Function in life: important for
the action of certain enzymes
and for muscle contraction.
● Iron (Fe26)
○ Atomic mass: 55.8
○ % of human weight: Trace
○ Function in life: a constituent
of hemoglobin, the
oxygen-carrying molecules

Components
● Nitrogen - proteins and nucleic acids
● Phosphorus- part of cell membrane and of energy storage molecules
● Sulfur- structural component of most proteins
● Chlorine- component of digestive acid
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Bodily Fluids
● Sodium- the primary ion
● Chlorine- the major ion

Constituent of Bones
● Calcium and Phosphorus

Constituent of Hemoglobin
● Iron

Actions of Muscles/ nerves/ enzymes

● Calcium- action of nerves and muscle.
● Potassium- nerve action
● Sodium- nerve action
● Magnesium- certain enzymes and for muscle contraction

LIPIDS
● insoluble in water
● Non Polar /Hydrophobic or water-fearing/hating.
● Contains Hydrocarbons /Carbon-carbon or carbon-hydrogen bonds

Examples: Meat, Cheese, and Oil

Functions of Lipid
● Energy storage
● Protection
● Insulation
● Lubrication
● Hormone precursor
● Key component of the cell membrane

Categories of Lipids
● Fat
● Phospholipid
● Steroid
● Wax
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1. Fat
● Also called triacylglycerols or triglycerides
● Solid at room temperature
● Used by animals for insulation, protection, and long term energy storage.
● Example: lard and butter
● Storage of fats
○ Adipocyte- animal cells
○ Seed- plant cells

● Components of fats
○ Glycerol- organic compound with 3 carbons, 5 hydrogen, and 3 hydroxyl
groups.
○ Fatty Acid
■ building blocks of fat
■ Carboxyl group makes it an acid
■ attached to each of the three carbons of the glycerol molecule
■ with an ester bond through an oxygen atom.
● Palmitic acid
○ Saturated fatty acid derived from the palm tree.
● Arachidic acid
○ Derived from Arachis hypogea scientific name for groundnuts or
peanuts.

● Types of fatty acids

○ Saturated Fatty Acid
■ Single bond
■ Saturated with hydrogen
■ Packed tightly and are solid at room temperature
■ Example: butyric acid, stearic acid, and palmitic acid
■ Contribute to plaque formation in the arteries.

○ Unsaturated Fatty Acid

■ Oil
■ Hydrocarbon chain with a double bond
■ Liquid at room temperature
■ Example: oleic acid, olive oil, corn oil, canola oil
■ Help to lower the blood cholesterol levels.
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● Categories of Unsaturated Fatty Acids

○ Monounsaturated fat
■ One double bond in a molecule
■ oleic acid (olive oil, nuts, egg, and meat)
○ Polyunsaturated fat
■ More than one double bonds in a molecule
■ linoleic acid (canola oil, soybean, corn, and
seeds)

● Configuration of the Molecule around Double Bonds

○ Cis Fat
■ Hydrogen atoms are present in the same plane.
■ Good cholesterol.
■ Sources: avocado, nuts, fish, corn oil
○ Trans fat
■ Hydrogen atoms are present in two different planes
■ a bad cholesterol (cardiovascular diseases)
■ Sources: Cakes, cookies, french fries, fried chicken

2. Phospholipid
● Contain glycerol and two fatty acids.
● A phosphate group is attached to the third carbon and not the glycerol.
● Unsaturated fatty acid causes kink in tails

3. Steroid
● Composed of four fused rings of carbon with different functional groups
attached.
○ Cholesterol
■ precursor for the synthesis of other steroids.
■ Stabilizes the plasma membrane
■ regulates membrane fluidity.

○ Sex hormones
■ Responsible for the development of primary and secondary sex
characteristics.
■ Male hormone - Testosterone
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■ Female hormones - Progesterone and Estrogen

○ Adrenocorticoid hormones
■ Aldosterone
● regulates the reabsorption of sodium and chloride ions
● kidney tubules.
■ Cortisol
● increases glucose and glycogen concentration

4. Wax
● Found in protective coatings on leaves and outer surfaces of animals.
● Prevent excessive water loss in plants.
● Produces in the ears of some animals to protect the eardrum.
● Nonpolar and repel water.
● Esters made of an alcohol chain and a fatty acid chain.

PROTEINS
● A large, complex molecule composed of many amino acids.
● Amino acids - monomers that comprise protein.

Types of Protein
● Enzyme
○ May help in breakdown, rearrangement, or synthesis reaction.
○ Salivary amylase which hydrolyses its substrate amylose, a component of a
starch.
● Hormones
○ Chemical- signaling molecules secreted by endocrine cells
○ control or regulate specific physiological processes
○ growth, development, metabolism, and reproduction
○ Insulin- regulates the amount of glucose in the body.

Functions of Protein
● Movement
○ Actin and myosin, necessary for contraction of muscle fibers
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● Structure
○ Keratin
■ forms hair, nails, horns, feathers, and scales.
○ Collagen
■ the most abundant protein in the human body,
■ Forms bones, tendons, ligaments, and cartilage.
● Transport
○ Hemoglobin in RBC carries oxygen
● Nutrition
○ Casein in milk stores amino acids for use by some newborn animals.
● Defense
○ Antibodies help animals fight off invasion by viruses and bacteria.
● Regulation
○ Enzymes help control chemical reactions in the body

Components of amino acid:

● a central carbon atom
● amino group (-NH2)
● carboxyl group (COOH)
● hydrogen atom
● side chain (R-group)

● Side chain (R) will identify the type of amino acid and give its nature whether it is
acidic, basic, polar, or non-polar.
● Peptide bond- bond between amino acids

Classification of Amino Acids

● Essential Amino Acids
○ Not naturally produced by the body.
○ Obtained through consumption of foods rich in protein.
○ Examples: isoleucine, leucine, lysine, methionine, phenylalanine, threonine,
tryptophan, and valine.
● Non-Essential Amino Acids
○ Naturally produced by the body.
○ Example: alanine, asparagine, aspartic acid, cysteine, glutamic acid,
glutamine, glycine, proline, serine and tyrosine.
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Chemical Nature of Amino Acids Determined by the R Group

● Aliphatic R groups (Nonpolar)
○ Alanine ● Charged R groups (Polar)
○ Isoleucine ○ Positively Charged (Basic)
○ Glycine ■ Lysine
○ Leucine ■ Arginine
○ Methionine ■ Histidine
○ Proline ○ Negatively Charged (Acidic)
○ Valine ■ Aspartate
● Uncharged R groups (Polar ) ■ Glutamate
○ Asparagine ● Aromatic R groups (Nonpolar)
○ Cysteine ○ Phenylalanine
○ Glutamine ○ Tyrosine
○ Serine ○ TryptophaN
○ Threonine

Protein Structure
● Primary Structure
○ The number and sequence of the amino acids found in the protein.
○ Linear sequence of amino acids.
○ Slight change can change the entire protein.
○ Sequence determines the function of protein.
○ Sickle cell anemia– glutamic acid replaced by valine (RBC become rigid,
sticky, and shaped like a crescent)
● Secondary Structure
○ Coil and spiral ■ Parallel strand of
■ H-bond polypeptides
■ Flexible and elastic ■ H-bond
■ Example: Hair and wool ■ Flexible but not elastic
■ Example: Silk (spider
web)
○ Beta pleated sheet
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● Tertiary Structure
○ Folding and bending of the coils
○ Three-dimensional complete folding pattern of the protein
○ 1 individual subunit (interaction among R groups) (like charges repel and
unlike charges attract in polar and nonpolar; so hydrophobic will be in the
inside and hydrophilic at the outside).
● Quaternary Structure
○ Multiple subunits (interaction of subunits or several polypeptides)
○ Protein consisting of more than one amino acid chain

Protein Denaturation- loss of biological activity

● Reversible Denaturation
○ Mild
○ Can be restored to its original conformation
○ Example: Hair rebond

● Irreversible Denaturation
○ Drastic
○ Protein will coagulate or precipitate from solution
○ Example: Fry egg (White)

Reagent Causing Denaturation

● Heat
● Microwave radiation
● UV radiation
● Violent whipping or shaking
● Detergent
● Organic solvent (ethanol, acetone, z-propanol) – denature bacteria
● Strong acids and bases (hydrolysis of peptide bond)
● Alkaloidal reagents – tannic acid and picric acid
● Guava leaves- rich in tannic acid. If in contact with an open wound, it would kill a
bacterial cell.

Renaturation
● Reagent will regain native structure and their biological activity (function)
● Denaturants were removed, the denatured proteins will fold back to native
conformations.
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NUCLEIC ACIDS
● store information which determine the type and structure of all specific proteins
● Polymers made up of nucleotides (monomers).

Nucleotide
• Phosphate molecule
• Pentose/ Sugar
• Nitrogenous bases

Bonds
● Covalent Bond
○ Bond between the 3 components of nucleotides.
● Phosphodiester Bond
○ Linked nucleotides together to form nucleic acid.

Nitrogenous Bases
● Purine (double ring)
○ Adenine
○ Guanine
● Pyrimidine( single ring)
○ Cytosine
○ Thymine (DNA)
○ Uracil (RNA)

2 Kinds of Nucleic Acids

● Deoxyribonucleic Acid- Carries instructions that control the activity of the cell
● Ribonucleic Acid- Uses the instruction from the DNA to make proteins.

Structure of DNA
● Discovered by James Watson and Francis Crick.
● Base pair and sugar phosphate backbone
● Double helix or spiral molecule
● Backbone runs antiparallel
● Nitrogenous bases
○ A doubled bonded with T
○ C triple bonded with G
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● Hydrogen bond between bases

Types of RNA
● Messenger RNA (mRNA)
○ transmits genetic instruction coded in the DNA
○ inside the nucleus to the cytoplasm particularly in the ribosome.
● Transfer RNA (tRNA)
○ Found in the cytoplasm of the cell
○ translates the codon of the mRNA into amino acids
○ attaching amino acids to the ribosomes facilitating protein synthesis.
● Ribosomal RNA (rRNA)
○ The protein factory of the cell
○ abundant in the cytoplasm

DNA RNA

Sugar

Strand Double Single

Nitrogenous Bases A, T, G, C A, U, G, C

Location nucleus cytoplasm

Function Carries genetic Involved in protein

information synthesis.

● Genetic code- gives instructions on what protein will be produced.

● Genotype- material found in the nucleus.
● Phenotype- observable characteristics when genotype was expressed.
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CENTRAL DOGMA OF MOLECULAR GENETICS

1. REPLICATION: HOW DNA COPIES ITSELF

● Unwinding
○ DNA helicase breaks the hydrogen bonds between nucleotides.
● Base Pairing
○ DNA primase adds the new nucleotides.
○ DNA polymerase does the proofreading to avoid mistakes.
● Joining
○ DNA ligase seals any breaks in the new DNA
strand.

2. TRANSCRIPTION: MAKING WORKING COPIES OF THE

GENES
● RNA polymerase
○ unzips the base pairs.
● The mRNA bases
○ pair up with existing DNA bases.
● The mRNA leaves the nucleus.

3. TRANSLATION: MAKING THE PROTEIN

● mRNA attaches to the ribosome
● tRNA attaches to the mRNA
● Anticodon pairs with codons of the mRNA and brings amino acids.
● Amino acids are joined by peptide bonds to form
proteins.
● Codon- The three-base code in the mRNA.
● Anticodon- The bases in the tRNA.
● AUG- start codon of methionine
● UAG- end codon of methionine
● AUG, UAA, UAG, UGA - end codon