Proteins Flashcards

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1
Q

draw a basic structure of an amino acid and label the different parts

A

-amino group
-carboxyl group
-variable group

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2
Q

draw the reaction between 2 amino acids

reaction? products? bond?

A

-condensation reaction
-water and dipeptide
-peptide bond

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3
Q

what is the primary structure of protein?

A

-the order/sequence of amino acids n the polypeptide chain joined by peptide bonds
-determines shape and function of protein
-around 20 different amino acids making different combinations

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4
Q

what is the secondary structure of protein?

A

-coiling or folding of amino acid chain due to hydrogen bonds
-alpha helix or beta pleated sheets
-hydrogen bonds between c=o carboxyl group of one and H of amino group of the other

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5
Q

what is the tertiary structure of protein?

A

-precise/functional shape, further folding of protein
-globular or fibrous

bonds:
-ionic - R group charged
-disulphide bridges if sulfur in R group present
-hydrogen bonds
hydrophilic or hydrophobic

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6
Q

what is the order of bonds/interactions in tertiary structure according to strength?

A

disulphide-ionic-hydrogen-hydrophilic/phobic

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7
Q

what is the quaternary structure of protein?

A

-a protein made up of more than one polypeptide chains
-e.g haemoglobin or collagen

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8
Q

-what is a prosthetic group?
-give an example

A

-a non protein associated with a protein
-e.g haem group in haemoglobin

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9
Q

compare fibrous and globular protein

A

Fibrous:
-regular repetitive sequence
-usually insoluble due to hydrophobic groups
-very strong
-cross linking of polypeptides chains by hydrogen bonds = fibrous structure
-collagen, elastin, keratin

Globular:
-tend to roll up into almost sphere
-soluble as hydrophilic groups outside on the surface
-much weaker secondary and tertiary bonds = denature
-polypeptide chains are folded in to form their specific shapes
-enzymes, hormones, insulin, haemoglobin

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10
Q

describe collagen a fibrous protein
and its function

A

-fibrous tight triple helix made of three polypeptide chains
-insoluble
-glycine - 1/3 of amino acid= polypeptides can wind tightly round as glycine is the smallest R group.
-no prosthetic group
-mainly left handed helix, triple helical

Functions:
-artery walls prevented from bursting
-tendons and ligaments connecting muscles to bones stretch without snapping
-bones- collagen network hardened
-cartilage and connective tissue

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11
Q

describe haemoglobin a globular protein
and its functions

A

-four polypeptide chains
-globular/round
-soluble
-made of many amino acids
-mainly alpha helix
-carry oxygen around the body
-haem prosthetic group

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12
Q

what is the test for protein?

A
  1. add biuret
  2. positive test goes from blue to purple/lilac
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13
Q

describe function and structure of insulin

A

-plays a role in blood glucose regulation
-two polypeptide chains linked by disulfide bonds
-bind to specific receptor molecules e.g glycoprotein on outside of muscle and fat cells to increase uptake of glucose from the blood

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14
Q

describe the function and structure of pepsin

A

-one polypeptide chain, has many acidic R groups to withstand acidic conditions in stomach
-protein digesting enzyme to make amino acids made in the stomach

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15
Q

describe the function and structure of keratin

A

-contains very high proportion of cycteine so lots of disulphide bridges
-hydrogen bonding making it very strong
-skin hair and nails where it provides mechanical protection and impermeable barrier to infection and water

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16
Q

describe the function and structure of elastin

A

-in blood arteries so can stretch and recoil
-crosslinking and coiling make it strong and extensible