Proteins Flashcards

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1
Q

what is amino acid

A

monomers from which proteins are made

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2
Q

draw the general structure of amino acids

A
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3
Q

what does the NH2 represent

A

amino group

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4
Q

what does the COOH represent

A

carboxyl group

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5
Q

what does R group represent

A

variable group ( 20 options of amino acids)

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6
Q

describe how the amino acids are joined together to form a dipeptide

A

via a condensation recation
results in the release of water
a peptide bond is formed between the OH in carboxyl group and H in amino group

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7
Q

what are proteins

A

polymers made up of the monomers amino acid

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8
Q

what are the four levels of structure in protein

A

primary
secondary
tertiary
quaternary

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9
Q

describe the primary structure

A

the order/sequence of amino acids in a protein

contains the initial sequence of amino acids and so therefore determine the proteins functions in the end

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10
Q

describe the secondary structure

A

-the shape that the chain of amino acid makes into either

-alpha helix or beta pleated sheet

-hydrogen bonds hold the secondary structure
-hydrogen bonds formed between the C=O groups of the carboxyl group of one amino acid and H in the amino group of the second amino acid.

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11
Q

when is a dipeptide formed

A

when two amino acids join together via a condensation reaction

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12
Q

when is polypeptide formed

A

two or more amino acids join together via a condensation reaction

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13
Q

what are proteins made of

A

one or more polypeptides

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14
Q

when does hydrolysis happen

A

when the polypeptide and dipeptides are broken down

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15
Q

describe the tertiary structure

A

-further folding of the secondary structure
-leads to form a unique 3D shape
-held in place by ionic , hydrogen and disulphide bridges

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16
Q

where are the bonds formed in the tertiary structure

A

-ionic and disulphide bonds form between the R groups of different amino acids

-Disulphide bonds only sometimes occur as there must be a sulfur in the R groups for this bond to occur (e.g, S—S)

17
Q

compare and contrast the bonding in the secondary and tertiary structures of a protein(2)

A

both secondary and tertiary contains hydrogen bonds whilst tertiary further contains ionic and disulphide bridges

18
Q

explain why the tertiary structure of proteins is important for metabolic reactions (3)

A

-enzymes are proteins that catalyse biological reactions
-the tertiary structure affects the shape of the enzymes active site
the active site must be complementary to the shape of the substrate in order to catalyse the reaction.

19
Q

define the quaternary structure

A

(protein made up of more than one polpeptide chain held together by bonds )

20
Q

example of a quaternary structure

A

haemoglobin

21
Q

Haemoglobin is the oxygen-carrying molecule in red blood cells. At low pH, haemoglobin’s ability to bind to oxygen is reduced.

Suggest why a low pH affects haemoglobin in this way.

A

interfers with the bonds in the haemoglobin causing it to change shape
means it can no longer bind onto the oxygen

22
Q

describe the importance of the primary structure and its impact

A

if one amino acid in the sequence is different then it will cause the ionic, hydrogen / disulphide bonds to form in a diff location

Impact:
-Enzymes will have a different active site shape ( non functioning)
-carrier proteins will have a diff shaped binding site ( so molecules are no longer complementary + so cannot be transported across membranes

23
Q
A