biological molecules 3

Question 1

what are amino acids

Answer 1

monomers of protiens

Question 2

what is a protien made from

Answer 2

more than 2 polypeptides

Question 3

define dipepetide and polypetide

Answer 3

dipepties are 2 amino acids and poly is more than 2

Question 4

draw the basic structure of an aminoacid

Question 5

what is the water molecule formed by condensation

Answer 5

peptide bond

Question 6

define the primary stage

Answer 6

the sequencing of amino acids in a polypeptided

Question 7

define the secondary stage

Answer 7

folded into either alpha helix( coiled structure)or beta pleated(see book)
and hydrogen bonds are made to hold the structure

Question 8

define the teriatry stage

Answer 8

folded more, more bondas added like hydrogen, ionic and maybe disulfide

Question 9

where are the ionic and disulfide bonds in between

Answer 9

inbetween the R groups

Question 10

what are disulfide bond

Answer 10

bond formed between r groups with sulfur in

Question 11

define the quatenary stage

Answer 11

proteins are made our of more than one polypeptide

Question 12

what happens to denatured protiens

Answer 12

lose 3d shape ad the bond breah apart

Question 13

why is sequencing important

Answer 13

it determines the placing of the bonds with determines the shape

Question 14

what are enzymes?

Answer 14

-biological catalyst
-type of protien
-help with digestion and respiration
-effect structure and functions
-intracelluar and extracelluar
-specific beacuse of tertairy structure

Question 15

what is an enzyme sbustrate complex?

Answer 15

when an active site is complemtary to a substrate, meaning they match in order to catalyse a reaction

Question 16

how do the speed up a reaction?

Answer 16

-supply a certain amount of energy before the reaction can start
-activation energy is heat
-enzymes lower activation energy to reactions can happen at alower temperature

Question 17

enzyme substrate complex

Answer 17

-when 2 substartes join, enzymes hold them togther which reduce replusion(easier)
- when catalysing a reaction, active site strains around the subsrate causing to to break easily

Question 18

what is lock and key

Answer 18

a simplified method which is the idea that an active site is a specific shape for s specific substrate

Question 19

what is induced fit

Answer 19

idea that an active site can be moulded around a substrate creating an enzyme substarte complex, the strain on the substarte cause by the active site is who the reaction is catalysed cauing it to break into its products.

Question 20

Enzyme properties

Answer 20

-related to their tertairy structure(which is determiined by the sequencing from there primary structure)
-very specifice, only catalyse one reaction- complemetary structure
-if the active site doesnt match the substarte and enzymesubstarte complex cant be formed and therfore the reaction wont be catalysed

Question 21

what are the 4 factors effecting enzyme contolled reactions?

Answer 21

-temperature
-ph
-substrate concentration
-enzyme concentration

Question 22

How doe temp effect it?

Answer 22

low temp, not enough kinetic energy, few collisons
high temp, more sucessful collisons, past optimum temp means enzymes denature and enzyme substrate complexs cant form
(bond break)

Question 23

ph?

Answer 23

too high(hydrogen) or low ph( to many OHminus) which intefere with the charge of amino acids which break bonds

Question 24

substrate concentration

Answer 24

insufficent substrate means that there are fewer collisons
more substrate - not enough enzymes (limiting factor)

Question 25

enzymes concentration

Answer 25

lack of enzymes- fewer collison
past optimum concentrate- active site will become saturated and plateau