Download Molecules of Life Review Topics

CP BIOLOGY
Chapter 2 Review
BIOMOLECULES
Name __________________
These are topics and vocabulary terms covered in this chapter which may appear on the chapter
test. See chapter guide, warm-ups, quick reviews, and text chapter 2 parts 3-4
Organic and inorganic – how different, recognize examples
The carbon atom and carbon skeleton






Valence electrons, # covalent bonds
Carbon chains – variety of shapes, branching, rings
Hydrocarbons – carbon and hydrogen only
Monomers – link in chains to form polymers
Dehydration synthesis (condensation)
o Joins molecules together, removes water
Hydrolysis – breaks molecules apart, adds water
Carbohydrates – functions - mostly energy 4 cal/gram
 Elements, ratio of H to O 2:1
 Monosaccharides - simple (single) sugars
o Glucose,fructose, galactose – isomers, all have 6 carbon atoms
 Disaccharides – double sugars; glucose + one other monosaccharide
o Sucrose, lactose, maltose

Polysaccharides – long chains of glucose molecules
o Energy storage - starch in plants, and glycogen in animals
o Structure – cellulose (fiber) in plants
Lipids – elements CHO – no ratio, functions – concentrated energy 9 cal/gram
 Monomers: glycerol and fatty acid, structure of each
 Triglyceride – which monomers, how many of each
 Saturated and unsaturated – how different, where found
o Hydrogenated and trans fat – what are they? Why important?
 Heart and blood vessel health
o Atherosclerosis, angioplasty
 steroids – cholesterol, sex hormones, cortisone
 phospholipids – what are they, where found
CP BIOLOGY Chapter 2 Review
Name __________________
PROTEINS, ENZYMES, and NUCLEIC ACIDS
These are topics and vocabulary terms for proteins, enzymes and nucleic acids. See chapter guide, warm-ups,
quick reviews, and text chapter 2 parts 3-4 for additional review.
Proteins – elements C H O N
 functions: structure, transport, defense, movement, messengers, catalysts
 monomer – amino acid: carbon, amino, carboxyl, H and variable (R group)
 R group – how many – 20; important – cross links hold 3-D shape of protein
 Peptide bond- covalent, between amino acids
 Dipeptide, polypeptide – how is a protein different? – 3-D shape
 Levels of structure
o Primary structure – sequence of amino acids
o Secondary and tertiary – coiling and folding into 3-D shape, one chain
o Quaternary – two or more polypeptides together
 Denature – what is it? – protein unfolds; What happens? – loses function
o Caused by? – temperature, pH, electrolytes (ions)
 Sickle cell disease – why is shape important?
Enzymes –What are they? – protein catalysts Why important? – speed reactions in cells
 Activation energy – needed to start a reaction, enzymes make it lower
 Active site and substrate – what are they?
 Modes of enzyme action – lock-and-key, induced fit
 Conditions that affect enzyme action
o Temperature – warm increases rate; hot denatures protein
o pH – narrow range for best pH, excess H+ or OH- break 3-D bonds
o concentration of enzyme or of substrate – act like a limiting reagent
o inhibitors – slow enzyme action: competitive – on active site;
 noncompetitive – somewhere else on enzyme
 feedback – a product of the reaction acts as inhibitor
Nucleic Acids – elements – C H O N P
 function DNA – store genetic information, function RNA – use DNA code to make protein
 what is a gene? – section on one strand of DNA, has instructions for one trait
 monomer – nucleotide: 3 parts- sugar, phosphate group, nitrogen base
 DNA and RNA - how different?
o DNA double helix; RNA single strand;
o DNA deoxyribose sugar; RNA ribose sugar
o DNA thymine base, and adenine, cytosine, guanine;
o RNA – uracil base, and ACG
 ATP – energy molecule, nucleotide with three phosphate groups