biological molecules 3 Flashcards
what are amino acids
monomers of protiens
what is a protien made from
more than 2 polypeptides
define dipepetide and polypetide
dipepties are 2 amino acids and poly is more than 2
draw the basic structure of an aminoacid
what is the water molecule formed by condensation
peptide bond
define the primary stage
the sequencing of amino acids in a polypeptided
define the secondary stage
folded into either alpha helix( coiled structure)or beta pleated(see book)
and hydrogen bonds are made to hold the structure
define the teriatry stage
folded more, more bondas added like hydrogen, ionic and maybe disulfide
where are the ionic and disulfide bonds in between
inbetween the R groups
what are disulfide bond
bond formed between r groups with sulfur in
define the quatenary stage
proteins are made our of more than one polypeptide
what happens to denatured protiens
lose 3d shape ad the bond breah apart
why is sequencing important
it determines the placing of the bonds with determines the shape
what are enzymes?
-biological catalyst
-type of protien
-help with digestion and respiration
-effect structure and functions
-intracelluar and extracelluar
-specific beacuse of tertairy structure
what is an enzyme sbustrate complex?
when an active site is complemtary to a substrate, meaning they match in order to catalyse a reaction
how do the speed up a reaction?
-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
enzyme substrate complex
-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
what is lock and key
a simplified method which is the idea that an active site is a specific shape for s specific substrate
what is induced fit
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.
Enzyme properties
-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
what are the 4 factors effecting enzyme contolled reactions?
-temperature
-ph
-substrate concentration
-enzyme concentration
How doe temp effect it?
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)
ph?
too high(hydrogen) or low ph( to many OHminus) which intefere with the charge of amino acids which break bonds
substrate concentration
insufficent substrate means that there are fewer collisons
more substrate - not enough enzymes (limiting factor)
