Know chemistry vocabulary (review packet) Difference between
types of bonds and how many bonds elements form (CHNOPS) hydrogen
(weak bonds between molecules) ionic (lose electron) covalent
(share electrons) polar v. nonpolar molecules
Slide 3
polar molecule...results in v shape know properties of water
(cohesion, adhesion, surface tension) high heat capacity solid less
dense than liquid (ice floats) know differences between solution,
solute, solvent, aqueous solution; hydrophilic and hydrophobic
Water is an excellent solvent. Ionic and polar substances dissolve
easily in water nonpolar substances do not dissolve in water Acids,
bases, pH and buffers **Think about all of these concepts in terms
of living systems. How do all of these concepts allow a living
organism to function? or cause an organism to not function
successfully?
Slide 4
Carbon is the most important element in living things.
Carbon-based life forms Carbon has the ability to make 4
bonds...resulting in incredible versatility in bonding with other
elements (it can make large, complex molecules) Hydrocarbons
(carbon and hydrogen only)--fossil fuels Isomers (structural v.
geometric) Structural- differ in covalent arrangement of atoms
Geometric- differ in spatial arrangements Enantiomer- mirror images
can form branches, chains and rings
Slide 5
polymer--long molecule made of smaller building blocks
carbohydrates, proteins, nucleic acids. **lipids**
monomer--building blocks that make up polymers synthesis of
polymers dehydration reactions--covalent bonds between molecules
with the loss of a water molecule breakdown of polymers
hydrolysis--molecules are broken using water (reverse of
dehydration rxn) enzymes: macromolecules that speed up chemical
reactions
Slide 6
Functional Groups--chemical groups attached to carbon skeleton
that determine function and unique properties of large molecules
Figure 4.9 testosterone vs. estradiol
Slide 7
Functional Groups Each has specific chemical properties, when
attaches to larger molecule it gives those properties to that
molecule A single molecule may contain many different functional
groups Determines molecular shape and reactivity Hydroxyl (-OH)
Alcohols Polar Hydrogen bond with water Carbs, proteins, nucleic
acids and lipids
Slide 8
Carbonyl (-CO) ketones and aldehydes Component of sugars
Carbohydrates, nucleic acids Carboxyl (-COOH) important part of
amino acids organic acids (ie. vinegar) Proteins, lipids Amino (-NH
2 ) important part of amino acids Basic (H+ acceptor) Proteins,
nucleic acids
Slide 9
Sulfhydryl (-SH) present in certain amino acids (methionine and
cysteine) Forms disulfide bridge (protein structure) proteins
Phosphate (-OPO 3 ) part of cellular energy sources (ATP, ADP)
Acidic Nucleic acids Methyl (-CH 3 ) part of DNA molecules (gene
expression) proteins
Slide 10
Have the general formula C n H 2n O n Functions Source of
stored energy Used to transport energy Structural molecules Used as
building blocks for other macromolecules Recognition or signaling
molecules that trigger specific responses
Slide 11
Monosaccharide: simple sugar Pentose sugar (5 carbon) C 5 H 10
O 5 Ribose, deoxyribose Hexose sugar (6 carbon) C 6 H 12 O 6
Glucose**, fructose, galactose (isomers) Fructosefruit sugar, very
sweet! Example of how arrangement of carbon atoms change molecule
properties
Slide 12
Polysaccharide: polymer of monosaccharides Formed by glycosidic
linkages (covalent bond that results from dehydration reactionlose
H 2 O) sugar bond Sucrose (glucose + fructose)disaccharide Used in
carbohydrate transport Lactose (glucose + galactose)disaccharide
Milk sugar Some individuals are missing the enzyme to break down
this sugarlactose intolerance
Slide 13
Starch (glucose+ glucose+ glucose.) Storage polysaccharide
(plants) Molecules broken by hydrolysis for energy Long chain of
alpha-glucose molecules Glycogen-- highly branched polymer of
alpha-glucose Storage polysaccharide (animals) in liver and muscles
animal starch Celluloseunbranched polymer of beta-glucose
Structural polysaccharide (plant cell wall) Not easily broken down
by most organisms Herbivores have special bacteria to do this
Chitin (modified glucose chain) Structural material found in
arthropods (insects) and fungi Makes up exoskeletons
Slide 14
Group of molecules that are insoluble in water Hydrophobic May
be storage fats, oils, steroids, or waxes Important component of
cell membranes Phospholipids (phosphate attached to glycerol) 2 FA
instead of 3 Polar and nonpolar ends of molecule (hydrophilic and
hydrophobic regions) Phosphate hydrophilic Serve as a long-term
form of energy storage Very efficient molecule for storage
Slide 15
Made of two components: Fatty acid tail of molecule Long chain
hydrocarbons with carboxyl group Chain is usually 14-20 carbons
long Glycerol head of molecule Three OH groups (hydroxyl) alcohol
Holds molecule together FA and glycerol held together by an ester
linkage Carboxyl + Hydroxyl
Slide 16
Triglyceride- one glycerol plus 3 FA (basic fat/oil) Saturated
FA No double bonds (carbon atoms) Maximum number of hydrogens Solid
at room temperature (animal fats-- butter) Unsaturated FA One or
more double/triple bonds (carbon atoms) Liquid at room temperature
(plant fats--oils) Monounsaturated (one double/triple bond)
Polyunsaturated (more than one double/triple bond) trans fats
partially hydrogenated unsaturated fats. Created by adding hydrogen
and breaking double/triple bonds (health risks)
Slide 17
Waxes Alcohol + unsaturated oil Steriods 4 carbon rings
Attached functional groups make them unique (testosterone vs.
estrogen) Ex. Cholesterol (component of cell membranes and
precursor to other steriods)
Slide 18
DNA and RNA Genetic information inherited from parents RNA used
in protein synthesis Polymers of nucleotides Sugar, phosphate,
nitrogenous base
Slide 19
Every dynamic function of an organism depends on proteins!
Functions include: (Fig. 5.15) Transport (hemoglobin) Structure
(collagen) Enzymes (trypsin) Movement (myosin) Defensive
(immunoglobin) Hormones (insulin) Storage (caesin)
Slide 20
Proteins are made of monomers called amino acids. 20 amino
acids exist in nature (fig. 5.16) Each has an amino and carboxyl
group Chains of amino acids are called polypeptides Amino acids are
linked together with a peptide bond Each polypeptide has an amino
group at one end and a carboxyl group at the other The unique
properties and structure are determined by the side groups of the
amino acid (unique to each a.a.)
Slide 21
A polypeptide chain becomes a protein once it has undergone
modification and folding (3-dimensional) The 3-D structure is
determined by the unique sequence of amino acids. (each protein is
folded uniquely) Four Levels (fig. 5.20) Primarychain of a.a. (not
folded) SecondaryH-bonds form between a.a. (making helix or pleated
sheet) Tertiary 3-D shape formed from reactions between a.a. side
chains (sulfide bridges) Quaternary multiple polypeptides (chains)
linked together in 3-D structure
Slide 22
Proteins exposed to excessive heat, pH changes, chemical, or
other environmental changes may change their shape and become
ineffective (misshapen)