Proteins Flashcards

(55 cards)

1
Q

What are proteins made up of?

A

Amino acids

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2
Q

What elements make up a protein?

A
C
H
O
N
(S)
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3
Q

How many naturally occurring amino acids are there?

A

20

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4
Q

What is the basic structure of an amino acid?

A
R 
                      I         
H  —  N  —  C  —  C  =  O 
           I          I         I 
          H        H        OH
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5
Q

How are 2 amino acids joined (functional groups) ?

A

Amino group of one

Carboxyl group of another

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6
Q

What type of reaction joins 2 amino acids?

A

Condensation

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7
Q

What is the bond name formed between 2 amino acids?

A

Peptide bond

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8
Q

What is the name of 2 amino acids joined together?

A

Dipeptide

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9
Q

What are the type of bonds which form the 3D structure of the protein?

A

Hydrogen bonds
Iconic bonds
Disulphide bridges

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10
Q

What do the type of bonds formed between amino acid chain depend on?

A

The R group

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11
Q

Which atoms form hydrogen bonds in amino acid chains?

A

Delta negative charge of O (lone pairs)

Delta positive charge of H

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12
Q

What affects hydrogen bonds?

A

Temperature

pH

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13
Q

Which 2 molecules allow the formation of disulphide bridges?

A

Cysteine molecules

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14
Q

How does a disulphides bridge occur?

A

Oxidation reaction between 2 sulfur groups

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15
Q

What is the primary structure of a protein?

A

The sequence of amino acids that make up the polypeptide chain help together by peptide bonds

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16
Q

What is the secondary structure of a protein?

A

The arrangement of the polypeptide chain into a regular repeating structure held together by hydrogen bonds

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17
Q

Give examples of secondary structure.

A

a helix

B pleated sheet

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18
Q

What type of protein is prone to having B pleated sheets as a secondary structure?

A

Fibrous proteins

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19
Q

What is tertiary structure?

A

A level of 3D organisation imposed on top of the secondary structure of many proteins

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20
Q

What type of protein is prone to having tertiary structures?

A

Globular proteins

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21
Q

What is the quaternary structure of a protein?

A

Only seen in proteins consisting of several polypeptide chains

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22
Q

Give examples of quaternary structure.

A

Important enzymes

Blood pigment haemoglobin

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23
Q

What is the name of changes in protein structure leading the bonds to break?

24
Q

What are the properties of fibrous proteins?

A

Little or no tertiary structure
Long parallel chains with occasional cross-linkages into fibres
Insoluble in water
Very tough

25
What is the function of fibrous proteins?
Structural proteins Appear in connective tissues Keratin in hair
26
Give an example of a fibrous protein.
Collagen
27
What is the function of collagen?
Gives strength to tendons, ligaments, bones and skin
28
What is the primary structure of collagen?
3 polypeptide chains Each up to 1000 amino acids long Repeating sequences of glycine and 2 other amino acids
29
Which amino acids make up collagen?
Glycine and 2 others | Often proline and hydroxyproline
30
How are the amino acids arranged in collagen?
Three a - chains are arranged in a unique triple helix | Held together by very large no of hydrogen bonds
31
What disease may result in the triple helix of collagen not forming?
Genetic disease osteogenesis imperfecta
32
What are the properties of globular proteins?
Complex tertiary (and sometimes quaternary) structure Spherical shapes Large size
33
Why are globular proteins insoluble?
They are too big
34
What is unusual about globular proteins solubility?
Is expected to dissolve in water (ionic properties of amino and carboxyl group) form a colloid instead
35
What is the name of the molecule formed by globular proteins in water?
A colloid
36
What is the function of globular proteins?
Hold molecules in position in the cytoplasm
37
Give examples of globular proteins.
Antibodies Enzymes Some hormones Haemoglobin
38
How is haemoglobin held together?
Disulphides bridge
39
What are conjugated proteins?
Protein molecules that join with/ conjugate to another molecule called a prosthetic group
40
Give an example of a conjugated protein (including the prosthetic group)
Haemoglobin (Iron containing prosthetic group) Chlorophyll (Magnesium containing prosthetic group)
41
What are glycoproteins?
Proteins with a carbohydrate prosthetic group
42
What is the problem with glycoproteins?
Carbohydrate part of molecule helps them hold lots of water makes it harder for protein digesting enzymes to break them down
43
Give examples of glycoproteins used in the body.
Lubricants - mucus and synovial fluid
44
Why are glycoproteins good lubricants?
Water holding properties make them slippery and viscous - reduces friction
45
What are lipoproteins?
Proteins conjugated with lipids
46
What is the role of lipoproteins?
Important in the transport of cholesterol in blood
47
What is the difference between HDLs and LDLs?
HDLs contain more protein - so they are denser
48
What are the types of lipoproteins found in blood?
High density lipoproteins | Low density lipoproteins
49
What is the test for proteins?
Biuret test | Blue solution —> purple solution
50
What are amino acids?
The building blocks of proteins
51
What is a peptide bond?
The bond formed by condensation reactions between amino acids
52
What are fibrous proteins?
Proteins that have long, parallel polypeptide chains with the occasional cross-linkages that form into fibres, but with little tertiary structure
53
What is a disulphide bridge?
A strong covalent bond formed as a result of an oxidation reaction between sulfur groups in cysteine
54
What are globular proteins?
Large proteins with complex tertiary and sometimes quaternary structures, folded into spherical (globular) shapes
55
What is a prosthetic group?
The molecule that is incorporated in a conjugated protein