1.4.1: Proteins Flashcards

1
Q

describe the general structure of an amino acid

A

amine group, r group, central carbon atom, hydrogen atom, carboxyl group

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2
Q

what is the general formula of an amino acid

A

NH2CH(R)COOH

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3
Q

what is the R group in an amino acid

A

variable group

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4
Q

how many different amino acids are there

A

20

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5
Q

what bond forms when there is a condensation reaction between amino acids

A

peptide bond

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6
Q

what type of reaction occurs between amino acids to form a peptide bond

A

condensation reaction

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7
Q

what molecule is removed and from which parts of the amino acids are they removed from a condensation reaction occurs between two amino acids

A

water is removed - OH from carboxyl group of one amino acid, H atom from amine group of the other amino acid

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8
Q

How can you tell where a polypeptide starts and finishes

A

start = N terminal (amine group)
end = C terminal (carboxyl group)

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9
Q

Describe what the primary structure of a polypeptide/protein is

A

number, type and sequence of amino acids in polypeptide chain

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10
Q

what are the bonds in the primary structure of a protein and where are they

A

peptide bonds between carboxyl group and amine group

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11
Q

Describe what the secondary structure of a polypeptide/protein is

A

twisting of the primary structure into a regular structure: either alpha helix or beta pleated sheet or both

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12
Q

what are the bonds in the secondary structure of a protein and where are they

A

hydrogen bonds between carboxyl group and amine group

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13
Q

Describe what the tertiary structure of a polypeptide/protein is

A

further folding of the secondary structure into a 3D globular shape

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14
Q

what are the bonds in the tertiary structure of a protein and where are they

A

hydrogen bonds between carboxyl group and amine group
ionic bonds or disulphide bridges between R groups

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15
Q

Describe what the quaternary structure of a polypeptide/protein is

A

functional protein composed of more than one polypeptide that may be secondary or tertiary in structure but not both

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16
Q

what two types of structure can fibrous proteins have

A

1 - one secondary polypeptide - functional protein
2 - multiple secondary polypeptides (quaternary structure) - functional protein

17
Q

what are two structural properties of fibrous proteins

A

high tensile strength
insoluble

18
Q

give 2 examples of fibrous proteins and their functions

A

Collagen - connective tissue e.g. ligaments
Keratin - hard tissue e.g. nails, hair, hooves

19
Q

what two types of structure can globular proteins have

A

1- one tertiary polypeptide - functional protein
2 - multiple tertiary polypeptides (quaternary structure) - functional protein

20
Q

what does the function of a globular protein depend on

A

function depends on specific 3D shape

21
Q

what are 2 properties of globular proteins

A

1 - soluble in water as their surface is hydrophilic and centre is hydrophobic
2 - hydrophobic R groups face inwards, hydrophilic R groups face outwards

22
Q

What is a conjugated protein and give an example

A

protein with non polypeptide group e.g. haemoglobin has a haem group

23
Q

what happens if you change the primary structure of an amino acid

A

a non functioning protein is produced

24
Q

what happens when a protein is denatured

A

change in shape - bonds breaking

25
Q

what are 2 causes of a protein denaturing and state the bonds that break

A

high temperature - H bonds break
extreme pH - ionic bonds break

26
Q

what is the impact on fibrous proteins if it is denatured

A

lose structural strength

27
Q

what is the impact on globular proteins if it is denatured

A

become inactive / insoluble