biology 1 : biological molecules - proteins and lipids Flashcards
what are lipids used for and where are they found
source a energy
oils and fats
waterproofing
reduce heat loss
triglycerides structure
1 glycerol with 3 fatty acids
what do fatty acids contain
carboxylic group
what does a molecule of gylcerol contains
3 hydroxyl
what happens when fatty acids and glycerrol react
form an ester bond
name the properties of trigylcerides
non polar - hydrophoic
contains alot of carbon and hydrogen so a lot of energy can be released
what is the structure of a phospholipid
phosphate head glycerol + 2 fatty acids
What is the difference between the head and the tail of a phospholipid
polar head
non polar tail
what is the structure of a amino acid
amine group(NH2)
carboxyl(cooh)
r group
whats is the bond called when amino acids react
peptide bonds
whats the difference between a polypeptide and a protein
need to fold into a complex 3d shape
what is the primary structure
sequence of amino acids in a polypeptide(helps determine the final 3d structure)
what causes the secondary structure
nh groups are slightly positive
co groups are slightly negative
they will attract each other and form hydrogen bonds
which causes it to twist into the secondary structure (alpha helix or beta pleated sheets)
what causes the teritary structure
beat pleated sheet and alpha helix being folded
what causes the formation of the quaternary structure
many polypeptides(subunits) working together
to form a larger 3d structure
what is it called when non protein molecules are formed at the quarternary structure
prosthetic groups
e.g(heam helps oxygen to bind)
what occurs during hydrogen bonding (hydroxyl)
due to a slight positive and negative charge on the hydroxyl
hydrogen bon will form
contributes the 3d shape of polypeptide chain
weak bonds
how does ionic bonding occur in proteins
between amino acids with charged r groups
r groups that are oppositely charged attract with each other
and form ionic bonds
only broken by changes in ph (reason why enzymes denature)
how does disulfide bonding occur
two molecules of cysteine(amino acids)
this contains a sulfur atom
sulfur atoms form a covalent bond
how can ionic bonds in proteins be broken
only broken by changes in ph (reason why enzymes denature)
how can disulfide bond be broken
they cant be broken down with temperature or ph
very strong
explain the induced fit model
complementary substrate causes
the tertiary structure of the active site to change and mould itself around the substarte forming a enzyme-substare complex
(bonds formed help catalyse the reaction)
enzyme-substrate complex formed
what happens in noncompetitive inhibition
bind to the allosteric site
causes tertiary structure to change(changes active site)
substrate no longer fits
(can not be overcome)
what happens in competitive inhibition
comeplementay to substrate
binds to active site
however its not permanent
increasing substate concentration reduces affect of it
name 6 ways that affect the rate of reaction
enzyme concentration
substate concentration
non competititve
competitive inhibitors
ph
temperature
How do you join two amino acids together
(H) in amine group bonds to (oh) in carboxyl group
Name all the bonds that make up the tertiary structure and it’s backbone
Disulfide
Ionic
Hydrogen
Backbone= polypeptide
