ap bio macromolecules exam

why carbon?

many ways to bond and natural formations

compounds with the same numbers of atoms but different structures

isomers

atoms that differ in covalent arrangement

structural isomers

covalent bonds to the same atoms but different spacial arrangement due to the inflexibility of double/triple bonds

cis-trans isomers

mirror image isomers

enantiomers

possible elements in carbohydrates

C, H, O

formations that are often a linear skeleton but may become cyclized in an aqueous solution

sugars

carbohydrate monomer

monosaccharide

carbohydrate polymer

polysaccharide

carbohydrate bond

glycosidic

2 roles of carbohydrates

structure and storage

structural roles of carbohydrates

strength, frame, load bearing

plant strength carbohydrate

cellulose

animal strength carbohydrate

chitin

storage role of carbohydrates

energy by storing glucose

animal storage carbohydrate

glycogen

plant storage carbohydrate

starch

cellulose, amylose, amylopectin source

plants

cellulose subunit

beta glucose

amylose, amylopectin, glycogen subunit

alpha glucose

glycogen source

animals

do cellulose and amylose branch

no

do amylopectin and glycogen branch

yes

how often does amylopectin branch

per 20 subunits

how often does glycogen branch

per 10 subunits

shape of cellulose

unbranched chains of cellulose fibrils

shape of amylose

helical and unbranched

shape of amylopectin

slightly branched and more soluble in water

shape of glycogen

highly branched and most soluble in water

what macromolecule does not form true polymers

lipids

what elements can lipids have

C, H, O, P

types of lipids

triglycerides, phospholipids, steroids, waxes

lipid component

fatty acids

fatty acids with only carbon-carbon single bonds

saturated fatty acids

fatty acids with at least one carbon-carbon double bond

unsaturated fatty acids

characteristics of saturated fatty acids

solid at room temp, pack tightly

characteristics of unsaturated fatty acids

liquid at room temp, can be cis/trans isomers, pack loosely due to kinks

converting unsaturated fatty acids to be saturated

trans fats

“plaque” forms on the outsides of blood vessels due to trans fats

artherosclerosis

functions of lipids

lightweight energy, cushions organs, insulates body, electrical insulator for neurons, speeds up transmission of electrical signals, makes up all cell membranes, helps absorbs vitamins ADEK, wax has structural and waterproofing

name of lipid insulator of neurons

myelin sheath

bond of lipids

ester

layer of phospholipids that make up a membrane

phospholipid bilayer

3 fatty acid molecule

triglyceride

2 fatty acid, 1 phosphate group molecule

phospholipid

base molecule of steroids

cholesterol

cholesterol’s role in the cell membrane

can inc/dec fluidity by inserting itself between phospholipids

ways to optimize membrane fluidity

inc/dec ratio of saturated/unsaturated fatty acids or cholesterol

biological catalysts that accelerate biochemical reactions

enzymatic proteins

storage of amino acids

storage proteins

coordination of an organisms activities

hormonal proteins

movement within cell

contractile and motor proteins

protection against disease

defense proteins

transport of substances

transport proteins

response of cell to chemical stimuli

receptor proteins

support system in cell

structural proteins

ex. of storage protein

casein from milk

ex. of hormonal proteins

insulin

ex. of contractile and motor proteins

actin and myosin

ex. of defense proteins

hemoglobin

how do receptor proteins work

recieve signaling molecules from nerve cells

ex. of structural proteins

keratin in hair, horns, feathers, shells

unbranched polymers built from the same set of 20 amino acids

polypeptides

protein monomer

amino acids

possible elements in proteins

C, H, O, N, S

name of protein groups

carboxyl, amino, H, variable R

how many nonpolar side chains are there

9/20

how many polar side chains are there

6/20

how many charged side chains are there

5/20

protein bond

peptide

food with all four macromolecules and everything needed for growth and development

whole foods

unique sequence of amino acids from genetic inheritance

primary structure

coils and folds in the peptide chain resulting from hydrogen bonds in the backbone

secondary structure

helical secondary structure formed by hydrogen bonds parallel to helix axis

alpha helix

sheet of secondary structure formed by hydrogen bonds between polypeptide strands

beta sheets

structure determined by interactions between R groups

tertiary structure

strong covalent bonds that may reinforce protein structure

disulfide bridges

2 or more polypeptide chains form a single macromolecule

quaternary structure

protein shape…

determines function

ex of loss of protein shape

sickle cell disease

physical and chemical conditions can unravel protein structure ex…

pH, salt concentration, temperature

loss of a proteins native structure causing it to be biologically inactive

denaturation

protein molecules that assist the proper folding of other proteins

chaperonins

ex of diseases due to misfolded proteins

altzheimers, parkinsons

nucleic acid polymers

polynucleotides

nucleic acid monomers

nucleotides

components of a nucleotide

nitrogenous base, pentose sugar, phosphate group(s)

1 ring nitrogenous bases

pyrimidines

pyrimidine bases

cytosine, thymine, uracil

2 ring nitrogenous bases

purines

purine bases

adenine, guanine

end of a polynucleotide with an OH

3’ end

end of a polynucleotide with a phosphate group

5’ end

DNA functions

provides the directions for its replication, directs synthesis of mRNA, controls protein synthesis

nucleic acid bond

phosphodiester

deoxyribonucleic acid (DNA) sugar

deoxyribose

ribonucleic acid (RNA) sugar

ribose

structure of DNA

double helix

forces in DNA strand

hydrogen bonds between complementary bases, van der waals between stacked bases

blueprint for construction of a protein

messenger RNA mRNA