Proteins

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What is a dipeptide?
two amino acids joined together
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Define amino acids
Basic monomer units which combine to make a polymer called a polypeptide
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What is the general structure of amino acids?
Carboxyl group, R group, amine group, hydrogen
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How many types of natural amino acids are there?
20
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What group in an amino acid is variable?
R group
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What reaction combines amino acids to form dipeptides or polypeptides?
Condensation reaction
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What is released during a condensation reaction?
Water
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How is this molecule of water produced?
An -OH from one carboxyl group and an -H from an amine group
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What reaction breaks down a polypeptide?
Hydrolysis reaction (adding water)
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What bond is formed when amino acids combine?
Peptide bond
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What is the primary structure of proteins?
The unique order of the linear sequence of amino acids in a peptide or protein
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What bonds form in the secondary structure of proteins?
Hydrogen bonds
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What effect do these bonds have on a protein?
Causes it to coil into an alpha helix or fold into a beta pleated sheet
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What holds these structures in shape?
Hydrogen bonds
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Are hydrogen bonds weak or strong?
Weak
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What is the tertiary structure of proteins?
The irregular twisting and folding of a-helices of the secondary structure brought about by attraction and repulsion between amino acid side chains
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What attractive forces and bonds are there in the tertiary structure?
Electrostatic attraction between oppositely charged groups, hydrogen bond, ionic bonds and disulphide bridges
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How are disulphide bridges formed?
When the folding of the chain brings 2 R groups of the sulphur-containing amino acid cysteine close together and a disulphide bridge can be formed between them
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Disulphide bonds are strong. True/false
True
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Where are ionic bonds formed in the tertiary structure?
Between the carboxyl and amine groups that are not involved in forming peptide bonds
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What can easily break ionic bonds?
Changes in pH
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How many polypeptide chains are there in the Quaternary structure?
2 or more polypeptide chains
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Is this structure 3D?
Yes
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What are non-protein groups in the Quaternary structure called?
Prosthetic groups
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What is the prosthetic group in haemoglobin?
the iron containing haem group
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What determines the function of a protein?
It's primary structure (the sequence of amino acids)
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How is the structure of haemoglobin adapted to its function?
It is compact and soluble which makes it easy to transport. This makes it good for carrying oxygen around the body
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Why are globular proteins metabolic?
They are involved in chemical reactions
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Give three examples of globular proteins
Enzymes, receptors, membrane proteins, plasma proteins and antibodies
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How does their structure give them a water soluble layer?
Hydrophobic R groups face inwards while hydrophilic R groups are turned outwards
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Do globular proteins have a Quaternary structure?
Yes
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Are fibrous proteins soluble or insoluble?
Insoluble
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Do fibrous proteins provide structural support?
Yes
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How many polypeptide chains does haemoglobin contain?
4 (2 alpha chains and 2 beta chains)
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Is collagen soluble in water?
No
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Collagen is a globular/fibrous protein
fibrous
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How many polypeptide chains does collagen contain?
3
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Does collagen contain a prosthetic group?
No
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How does collagen form fibrils?
By forming covalent bonds (crosslinks) between collagen molecules which increases strength
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Other cards in this set

Card 2

Front

Basic monomer units which combine to make a polymer called a polypeptide

Back

Define amino acids

Card 3

Front

Carboxyl group, R group, amine group, hydrogen

Back

Preview of the back of card 3

Card 4

Front

20

Back

Preview of the back of card 4

Card 5

Front

R group

Back

Preview of the back of card 5
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