GENERAL BIOLOGY

Biomolecules

Carbohydrates AKA Saccharides

⁃ sugars and starches
⁃ made entirely of carbon, hydrogen, oxygen
⁃ for carbon; 18% of the body by weight, forms 4 covalent bonds, can form single or
double bonds or rings

Linear
⁃ carbon double bond oxygen, carbonyl

Ring
⁃ carbon must let go of one double bond to form a ring because carbon can only take 4
bonds

Monosaccharides
⁃ CH2O
⁃ carbonyl group (CO) and multiple hydroxyl groups (-OH)
⁃ cellular respiration
⁃ carbon skeleton serve as raw materials for synthesis of other types if small organic
molecules
⁃ Aldose (aldehyde sygar)
⁃ Ketose (ketone sugar)
⁃ carbon skeleton
◦ glucose (everywhere)
◦ fructose (fruits)
◦ galactose (as mono, peas)
◦ ribose (nucleic acids)
◦ deoxyribose (nucleic acids)

Classifying Sugars
⁃ location of carbonyl group, triose
◦ Aldoses - carbonyl group at the end of carbon section (e. x. glyceraldehyde)
◦ Ketoses - carbonyl group within carbon skeleton (e.x. fructose, dihydroxyacetone)
⁃ size of carbon skeleton
◦ glucose, galactose - aldoses, pentose
◦ fructose - ketose

Disaccharides
⁃ two monosaccharides joined by a glycosidic linkage, formed through dehydration
reaction
◦ sucrose = glucose + fructose (1-4 glycosidic linkage)
◦ maltose = glucose + glucose (1-2 glycosidic linkage) (e.x. pancakes, sweet potatoes,
french bread, fried onion rings, bagels)
◦ lactose = glucose + galactose (1-4 glycosidic linkage) through hydrolysis! (e.x. dairy
products)

Polysaccharides
⁃ complex carbohydrates
⁃ architecture and function; sugar monomers and positions of its glycosidic linkages
⁃ storage starch and glycogen
⁃ structural starch, cellulose

◦ starch - acts as a storage for plants; polymer of glucose monomers; joined by 1-4 linkage;
within cellular structures known as plastid; simplest form is amylose
◦ glycogen - liver, muscle and fat cells; systemic and cellular energy source
◦ cellulose - a major component of the tough walls that enclose plant cells; fiber; most
abundant organic compound on Earth
◦ chitin - major constituent in the exoskeleton of arthropods and the cell walls of fungi

Proteins
⁃ long chains (polymers) of subunits called amino acids (monomers), have 20 different
types, composed of amino end, carboxyl end, central carbon and R group, joined together by
peptide bonds (formed through dehydration synthesis)
⁃ carbonyl is a carbon double bond with oxygen
⁃ carboxyl is a carbonyl with a hydroxyl
⁃ bond between amino end and carboxyl group

Protein Structure
⁃ Polypeptide longer than 100 amino acids that has a complex structure and function
⁃ shape / structure of proteins is important because this determines how they interact with
other molecules and their particular function
Primary Structure
⁃ amino acid sequence stabilized by peptide bonds happens through transcription and
translation
⁃ dictates the secondary and tertiary structure
⁃ no function yet
Secondary Structure
⁃ how a polypeptide is oriented in space
⁃ alpha helix; right hand spiral formed between hydrogen bonds between regular interval
⁃ beta pleated sheets; formed by two primary structures that are adjacent to each other
(oxygen to hydrogen and hydrogen to oxygen)
⁃ stabilized by hydrogen bonds formed between the interactions of the polypeptide
backbones
⁃ Oxygen partially negative and Hydrogen partially positive
Tertiary Structure
⁃ three-dimensional shape; defines function
⁃ stabilized by (uncharged amino acids) hydrogen bonds, occasionally by iconic (charged
amino acids), disulfide bonds (cysteine or methionine) or hydrophobic interactions (cluster at the
core of the protein structure)
⁃ formed between interaction of side chains
⁃ created polar and non-polar areas in molecule
⁃ non-polar held by Van der Waals within the core of the protein
Quaternary Structure
⁃ two or more polypeptide chains are associated

Amino Acids
⁃ building blocks of proteins
⁃ contain nitrogen
⁃ 20 naturally occurring, 2 synthesized
⁃ R group determined chemical properties
⁃ half can be made by body, half need to be consumed
⁃ (e.x. phenylalanine, glycine, aspartic acid)
⁃ made in ribosomes, following DNA sequences
⁃ carbon, hydrogen, nitrogen, (sulfur)
⁃ carboxyl (carbon terminus) and amino group (nitrogen terminus) combined through
dehydration
⁃ Cysteine and Methionine have sulfur
⁃ some have Phosphorus because of DNA phosphate group
Peptide Bond
- forms between carboxyl end of one amino acid and amino end of the next amino acid
Polypeptide Bond
- a polymer of 3-100 amino acids

Denaturation
⁃ permanent disruption of protein structure
⁃ can be damaged by temperature of changes in pH
⁃ leads to loss of biological function
How we use proteins

How Our Body Uses Amino Acids as Building Blocks

⁃ amino acid -> peptide -> protein

Catalysts
⁃ speeds up the rate of the reaction (e.x. enzymes)
⁃ e.x. lipase and breaking down of fatty acids

Regulation (Hormones)
⁃ moderates the bodily functions
⁃ e.x. insulin regulates blood sugar
⁃ e.x. testosterone regulates male growth
⁃ e.x. estrogen regulates female growth

Structural
⁃ strengthens body structures
⁃ e.x. keratin for hair and nails
⁃ e.x. collagen from connective tissues
⁃ e.x. histone in DNA chromosomes

Transport
⁃ transfers molecules from one place to another
⁃ e.x. hemoglobin from blood for oxygen
⁃ e.x. channel protein or carrier protein

Immunity
⁃ defense
⁃ e.x. antibodies

Contractile
⁃ movement
⁃ e.x. actin and myosin

Surface Receptors
⁃ response to chemical stimuli that is sent to the cells

Enzymes
⁃ act as catalyst to accelerate a reaction
⁃ not permanently changed in the process
⁃ most enzymes are proteins (tertiary and quaternary)
⁃ work by weakening bonds which lowers activation energy (energy required by reaction to
push through)
⁃ specific and very specific and only work with certain substrates
⁃ specificity is based on the chemical properties of the active site and the chemical
properties of the substrate
⁃ they are not consumed by the reaction; temporarily used and then re-used for the same
reaction for the next substrate
⁃ very little enzymes are needed to help in many reactions
⁃ usually end in -ase

Enzyme-Substrate Complex
⁃ the substance (reactant) an enzyme acts on is the substrate
⁃ e.x. lactase for lactose -> glucose + galactose
⁃ Active Site; a restricted active region of an enzyme molecule which binds to the substrate

Induced Fit
⁃ a change in the shape of an enzyme's active site
⁃ induced by the substrate
1. Reactants approach enzymes
2. Reactants bond to enzymes
3. Enzyme changes shape
4. Product is created

What affects enzyme activity?

• environmental conditions
[] temperature
> optimum temperature (greatest number of collisions between enzyme and substrate)
> human enzymes (35-40 celsius) {37}
> higher temperature (boiling) may denature
> lower temperature (freezing) molecules move slower and there are less collisions
between enzyme and substrate)
[] ph
[] ionic concentration
• cofactors - inorganic substances (zinc, iron) and vitamins are sometimes needed for
proper enzymatic activity | e.x. iron must be present in the quaternary structure hemoglobin in
order for it to pick up oxygen; organic substances or coenzymes
• enzyme inhibitors - (e.x. poison, painkillers)
[] irreversible - covalent bond
[] reversible - ionic bond, add substrate
> competitive inhibitors - are chemicals that resemble an enzyme's normal substrate and
compete with it for the active site
> non-competitive inhibitors - inhibitors that do not enter the active site, but bind to another
part of the enzyme causing the enzyme to change its shape, which in turn alters the active site