Chapter 5 Study Guide
4 major groups of macromolecules
carbs, nucleic acids, proteins, lipids
dehydration vs. hydrolysis
what happens in each
when each is used
dehydration is used in polysaccharides, lipids, and proteins
a water molecule is removed
hydrolysis breaks a water molecule apart and its parts become attached to monomer. Breaks apart fats, proteins, and polysaccharides
steroids have multiple rings, with functional groups sticking out
chemical formulas and molecular structures for all carbs , lipids (3 types), proteins (primary and secondary structures)
carbs have a CHO ratio of 1:2:1, can tell molecular structure by numerous –OH
lipids have a CH ratio of 1:2, and only 2 oxygens, molecular structure has numerous C-H bonds
protein molecular structure – look for amino and carboxyl functional groups
monosaccharide, disaccharide, polysaccharide
number of molecules
examples of each type
mono- 1 molecule, glucose, fructose
di – 2 molecules, lactose
poly – many, cellulose, starch, chitin
starch vs. cellulose
why can’t humans digest cellulose
polymers of glucose
starch stores energy, alpha glycosidic linkages
cellulose used for structural purposes, beta glycosidic linkages
can’t digest b/can’t break down beta glycosidic linkages
facts about lipids
insoluable in water
makes components of cell membrane
stores 2x as much energy as glucose
triacylglycerol
made of 3 fatty acids and a glycerol
saturated fatty acid
no C-C double bonds
unsaturated fatty acid
one or more C- C double bonds
hydrogenation – what it does
decreases# of C-C double bonds
increases # of H atoms
at room temp, goes from oil to solid
saturated fatty acid vs. unsaturated fatty acid
solid at room temp / liquid at room temp b/c double bonds make kinks in structure
polypeptide
polymer of amino acids
parts of an amino acid
amino group, carboxyl groups, H, central carbon, and R group
what makes amino acids different from one another
The R group, or side chain
types of R groups ( polar, nonpolar, basic, acidic, hydrophobic, hydrophilic)
Hydrophobic R groups contain mostly C and H
peptide bonds – where formed
formed between carboxyl of one amino acid and the amino group of the next amino acid, one molecule of water is removed during bond
N terminus vs. C terminus
N – side by amino group
C- side by carboxyl group
Bonds in primary, secondary, and tertiary structures
Alpha helix, beta pleated sheets – where found
When are the interactions of R groups important
Purpose of disulfide bridges
Primary structure – peptide bonds
Secondary structure – hydrogen bonds, alpha helix, beta pleated sheets
Tertiary – 3-D shape of fully folded polypeptide
Disulfide bonds help maintain 3-D shape
Interactions of R groups happen at tertiary level
What happens to protein when 1 amino acid is changed
It can change primary and tertiary structures, and biological activity
Altering any of the structures can change the function of the protein
Examples of protein molecules form 5.4
Hemoglobin
Collegen
Transthyretin
lysozyme
Denaturation – what is it, what structure does it affect
A change in a protein’s 3-D shape or conformation due to disruption of H bonds, Ionic bonds, or disulfide bridges
Chaperonins
Molecules that insure the proper folding of a protein
Function of RNA
Function in the synthesis of protein
Pats of a nucleotide
5 carbon sugar, nitrogenous base, phosphate group
Purines vs. pryamidines
Purines – adenine and guanine, 2 rings
Pyramidiens – thymine, cytosine, uracil, 1 ring
A-T G-C
DNA bases vs. RNA bases
DNA – A, T, G, C
RNA – A, U, G, C
Differences between DNA and RNA
DNA - two strands, deoxyribose sugar, one less O than RNA
RNA – one strand, ribose sugar
What bonds hold the two sides of DNA together
Hydrogen bonds