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
what are 2 causes of a protein denaturing and state the bonds that break
high temperature - H bonds break extreme pH - ionic bonds break
26
what is the impact on fibrous proteins if it is denatured
lose structural strength
27
what is the impact on globular proteins if it is denatured
become inactive / insoluble