proteins Flashcards

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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
Q

what prosthetic group does haemoglobin have

A

haem group containing iron

26
Q

what kind of protein is haemoglobin

A

globular

27
Q

what is the function of insulin

A

hormone secreted by the pancreas

28
Q

what kind of protein is insulin

A

globular

29
Q

why is insulins solubility important

A

it means it can be easily transported by the blood

30
Q

describe the structure of insulin

A

two polypeptide chains held together by disulfide bonds

31
Q

what is the function of amylase

A

enzyme responsible for the breakdown of starch

32
Q

what is amylase made of

A

single chain of amino acids

33
Q

what is a fibrous proteins like

A

tough and rope shaped

34
Q

what are the main properties of fibrous proteins

A

insoluble and strong

35
Q

what kind of protein is collagen

A

fibrous

36
Q

where can collagen be found

A

in connective tissues- bone and muscle

37
Q

whats the main property of collagen

A

its strong

38
Q

what kind of protein is keratin

A

fibrous

39
Q

where can keratin be found

A

skin, hair, nails etc

40
Q

what 2 things can keratin be like

A

flexible or hard and tough

41
Q

what kind of protein is elastin

A

fibrous

42
Q

where can elastin be found

A

elastic connective tissue- skin, large blood vessels and ligaments

43
Q

why is elastin good

A

allows tissues to return to their original shape after being stretched

44
Q

Open does not form going to protein folds into its quaternary structure

A

Peptide bonds

45
Q

Explain the term conjugate of protein

A

Protein that contains nonprotein.
Prosthetic group
the prosthetic group is attached by covalent bonds

46
Q

Name the three main properties fibrous proteins have that globular proteins do not

A

Strong
Insoluble.
Unreactive.

47
Q

Describe the tertiary structure of a fibrous protein

A

It has little to none

48
Q

Name the chemical bond that links two cysteine amino acids

A

Disulphide bond

49
Q

It’s something only consist of a single polypeptide chain what structure will it not have?

A

Quaternary structure

50
Q

How are hydrogen ions useful in water?

A

They regulate the PH

51
Q

How is sodium irons useful in water?

A

They regulate the water potential

52
Q

Describe how the induced fit model of an enzyme works and have an enzyme acts as a catalyst

A

ESC forms
Active site changes shape so is complementary to substrate

Reduces activation energy

53
Q

Explain how active site of an enzyme causes high rate of reaction

A

Lois activation energy
Induced fit causes active site to change, shape
. Enzyme substrate complex