proteins Flashcards

1
Q

proteins are ——

A

polymers

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2
Q

what monomers make up proteins

A

amino acids

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3
Q

what is formed when two amino acids join together

A

dipeptide

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4
Q

what is formed when more then 2 amino acids join together

A

polypeptide

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5
Q

how many polypeptides make up a protein

A

one or more

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6
Q

name the 3 parts that make up an amino acid

A

amino group

variable ( r ) group

carboxyl group

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7
Q

what is the amine group made up of

A

NH2

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8
Q

what elements do all amino acids contain

A

carbon, oxygen, hydrogen and Nitrogen and some sulfur

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9
Q

what bonds link amino acids together

A

peptide bonds

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10
Q

what is a condensation reaction

A

reaction that releases a molecule of water and the hydroxyl group and a hydrogen are lost

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11
Q

what reaction breaks peptide bonds

A

hydrolysis

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12
Q

what is the primary structure of a protein

A

the sequence of amino acids in a polypeptide chain

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13
Q

what would a change in just one amino acid do

A

change the structure of the whole protein

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14
Q

what is the secondary structure of a protein

A

when polypeptide chains form alpha helix and beta pleated sheets

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15
Q

what is formed in the secondary structure of a protein

A

hydrogen bonds

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16
Q

what is the tertiary structure of a protein

A

the 3D structure due to further coiling of amino acids

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17
Q

what bonds can be found in the tertiary structure

A

ionic bonds

disulphide bonds

hydrophobic and hydrophilic interactions

hydrogen bonds

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18
Q

what is the quaternary structure of a protein

A

several polypeptide chains held together by bonds its the proteins final 3D structure

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19
Q

what do disulfide bonds form between

A

sulfur atoms

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20
Q

what is a globular protein like

A

round and compact

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21
Q

where are the r groups on a globular protein

A

on the outside

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22
Q

globular proteins are s—- why

A

soluble - so they are easily transported in liquids

23
Q

what is the function of haemoglobin

A

transports oxygen around the body in RBCs

24
Q

what is a conjugated protein

A

a protein with a non-protein group attached called a prosthetic group

25
what prosthetic group does haemoglobin have
haem group containing iron
26
what kind of protein is haemoglobin
globular
27
what is the function of insulin
hormone secreted by the pancreas
28
what kind of protein is insulin
globular
29
why is insulins solubility important
it means it can be easily transported by the blood
30
describe the structure of insulin
two polypeptide chains held together by disulfide bonds
31
what is the function of amylase
enzyme responsible for the breakdown of starch
32
what is amylase made of
single chain of amino acids
33
what is a fibrous proteins like
tough and rope shaped
34
what are the main properties of fibrous proteins
insoluble and strong
35
what kind of protein is collagen
fibrous
36
where can collagen be found
in connective tissues- bone and muscle
37
whats the main property of collagen
its strong
38
what kind of protein is keratin
fibrous
39
where can keratin be found
skin, hair, nails etc
40
what 2 things can keratin be like
flexible or hard and tough
41
what kind of protein is elastin
fibrous
42
where can elastin be found
elastic connective tissue- skin, large blood vessels and ligaments
43
why is elastin good
allows tissues to return to their original shape after being stretched
44
Open does not form going to protein folds into its quaternary structure
Peptide bonds
45
Explain the term conjugate of protein
Protein that contains nonprotein. Prosthetic group the prosthetic group is attached by covalent bonds
46
Name the three main properties fibrous proteins have that globular proteins do not
Strong Insoluble. Unreactive.
47
Describe the tertiary structure of a fibrous protein
It has little to none
48
Name the chemical bond that links two cysteine amino acids
Disulphide bond
49
It’s something only consist of a single polypeptide chain what structure will it not have?
Quaternary structure
50
How are hydrogen ions useful in water?
They regulate the PH
51
How is sodium irons useful in water?
They regulate the water potential
52
Describe how the induced fit model of an enzyme works and have an enzyme acts as a catalyst
ESC forms Active site changes shape so is complementary to substrate Reduces activation energy
53
Explain how active site of an enzyme causes high rate of reaction
Lois activation energy Induced fit causes active site to change, shape . Enzyme substrate complex