biology 1 : biological molecules - proteins and lipids Flashcards

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1
Q

what are lipids used for and where are they found

A

source a energy
oils and fats
waterproofing
reduce heat loss

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2
Q

triglycerides structure

A

1 glycerol with 3 fatty acids

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3
Q

what do fatty acids contain

A

carboxylic group

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4
Q

what does a molecule of gylcerol contains

A

3 hydroxyl

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5
Q

what happens when fatty acids and glycerrol react

A

form an ester bond

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6
Q

name the properties of trigylcerides

A

non polar - hydrophoic
contains alot of carbon and hydrogen so a lot of energy can be released

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7
Q

what is the structure of a phospholipid

A

phosphate head glycerol + 2 fatty acids

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8
Q

What is the difference between the head and the tail of a phospholipid

A

polar head
non polar tail

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9
Q

what is the structure of a amino acid

A

amine group(NH2)
carboxyl(cooh)
r group

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10
Q

whats is the bond called when amino acids react

A

peptide bonds

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11
Q

what happens when you join mant amino acids

A

polypeptide

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12
Q

whats the difference between a polypeptide and a protein

A

need to fold into a complex 3d shape

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13
Q

what is the primary structure

A

specific order of amino acids in a polypeptide(helps determine the final 3d structure)

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14
Q

what causes the secondary structure

A

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)

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15
Q

what causes the teritary structure

A

beat pleated sheet and alpha helix being folded

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16
Q

what causes the formation of the quaternary structure

A

many polypeptides(subunits) working together
to form a larger 3d structure

17
Q

what is it called when non protein molecules are formed at the quarternary structure

A

prosthetic groups
e.g(heam helps oxygen to bind)

18
Q

what occurs during hydrogen bonding (hydroxyl)

A

due to a slight positive and negative charge on the hydroxyl
hydrogen bon will form
contributes the 3d shape of polypeptide chain
weak bonds

19
Q

how does ionic bonding occur in proteins

A

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)

20
Q

how does disulfide bonding occur

A

two molecules of cysteine(amino acids)
this contains a sulfur atom
sulfur atoms form a covalent bond

21
Q

how can ionic bonds in proteins be broken

A

only broken by changes in ph (reason why enzymes denature)

22
Q

how can disulfide bond be broken

A

they cant be broken down with temperature or ph
very strong

23
Q

how do we know which bonds are in the tertiary structure

A

if they form between polypeptides on the same chain

24
Q

how do we know which bonds are in the quaternary structure

A

if they form between different sub units

25
Q

explain the induced fit model

A

complementary substrate causes
the tertiary structure of the active site to mould itself around the substrate(bonds are formed with amino acids)
(bonds formed help catalyse the reaction)
enzyme-substrate complex formed

26
Q

what happens in noncompetitive inhibition

A

bind to the allosteric site
causes tertiary structure to change(changes active site)
substrate no longer fits
(can not be overcome)

27
Q

what happens in competitive inhibition

A

comeplementay to substrate
binds to active site
however its not permanent
increasing substate concentration reduces affect of it

28
Q

name 6 ways that affect the rate of reaction

A

enzyme concentration
substate concentration
non competititve
competitive inhibitors
ph
temperature

29
Q

How do you join two amino acids together

A

(H) in amine group bonds to (oh) in carboxyl group

30
Q

Name all the bonds that make up the tertiary structure and it’s backbone

A

Disulfide
Ionic
Hydrogen
Backbone= polypeptide