1A-Proteins

Question 1

what monomer are proteins made of

Answer 1

amino acids

Question 2

what are amino acids general structure

Answer 2

a carboxyl group, amino group and a carbon containing R group (variable side group)
refer to pg 31

Question 3

how are amino acids linked together

Answer 3

by condensation reaction

Question 4

what is the bond between amino acids called

Answer 4

peptide bond
refer to pg 31

Question 5

what is the primary structure

Answer 5

sequence of amino acids in the polypeptide chains

Question 6

what is a secondary structure

Answer 6

polypeptide chain doesn’t remain flat and straight. hydrogen bonds form between amino acids in the chain making it coil into an alpha helix or a beta pleated sheet

Question 7

what is the tertiary structure

Answer 7

its coiled and folded further. more bonds form between different parts of the polypeptide chain (hydrogen and ionic bonds)
Disulfide bridges form whenever two molecules of amino acids cysteine bonds to the sulfur atom in the other. for proteins made from a single polypeptide chain the tertiary structure forms their final 3D structure

Question 8

what is a quaternary structure

Answer 8

the way these polypeptide chains are assembled together
for proteins made from more than one polypeptide chain the quaternary structure is the protien’s final 3D structure

Question 9

what is the biuret test for proteins

Answer 9

add a few drops of sodium hydroxide solution to make the solution alkaline
then add copper(II) sulfate solution
if present then solution turns purple otherwise it stays blue

Question 10

why are enzymes highly specific?

Answer 10

because of their tertiary structure

Question 11

what is the activation energy

Answer 11

certain amount of energy supplied to chemical before reaction starts

Question 12

what do enzymes do

Answer 12

they lower the activation energy to speed up the reaction

Question 13

what is an enzyme-substrate complex

Answer 13

when an substrate fits into the enzyme’s active site

Question 14

how does an enzyme-substrate complex lower the activation eneryg

Answer 14

because two substrate molecules that need to be joined will be held close together by the enzyme reducing repulsion between molecules so easier to bond
fitting in the active site puts a strain on the bonds in the substrate o substrate molecules will break more easily

Question 15

what is the lock and key theory

Answer 15

the substrate and active site have a complementary shape

Question 16

what is the induced fit model

Answer 16

where the substrate slightly changes the shape of the active site to fit even better.

Question 17

what are enzyme properties related to

Answer 17

their tertiary structure

Question 18

why are enzymes specific

Answer 18

becuause only complementary substrate will fit into the active site

Question 19

what determines the active site’s shape and how why does it mean a different active site

Answer 19

the tertiary structure each enzymes has different tertiary structure so different active site

Question 20

what would it mean if the tertiary structure of a protein is altered

Answer 20

shape of active site changes meaning substrate won’t fit into active site and enzyme-substrate complex won’t be made and enzyme will no longer be able to carry out its function.

Question 21

ways of altering the tertiary strucutre of an enzyme

Answer 21

temperature and ph

Question 22

what happens if a mutation occurs

Answer 22

primary structure of protein determined by gene if mutation occurs it could change tertiary structure of enzyme produced