The structure of proteins Flashcards

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1
Q

What elements do proteins contain?

A

Carbon, hydrogen, oxygen and nitrogen

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2
Q

How many different amino acids are found in cells?

A

20

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3
Q

Why are 5 of these 20 amino acids found in cells classified as non-essential?

A

Because our bodies can make them from other amino acids

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4
Q

How many amino acids can we only obtain from food? (and therefore are essential)?

A

9

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5
Q

Why are 6 of these 20 amino acids found in cells classified as conditionally essential?

A

because they are only required by infants and growing children

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6
Q

What part of the amino acid determines its type?

A

The R group

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7
Q

Draw the structure of an amino acid and label its different parts

A

d

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8
Q

Describe how two amino acids undergo a condensation reaction

A

The amine (-NH2) group of one amino acid and the carboxyl group (-OOH) of the other react and join to a central carbon atom. It is able to do this because the hydroxyl (-OH) in the carboxylic acid group (-OOH) reacts with one hydrogen atom in the amine group (-NH2) of the other amino acid. A water molecule (H20) is produced and a peptide bond is formed between the two amino acids

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9
Q

What is the name of the bond formed between two amino acids?

A

A peptide bond

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10
Q

What is always produced in a condensation reaction?

A

Water

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11
Q

What is the name of two amino acids joined together?

A

A dipeptide

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12
Q

What is the name of two or more amino acids that have joined together?

A

A polypeptide

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13
Q

What is the name of the enzyme that helps speed up the reaction for the condensation of amino acids?

A

peptidyl transferase

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14
Q

Where is peptidyl transferase found?

A

In ribosomes

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15
Q

What are ribosomes known for in regards to proteins?

A

Ribosomes are the site of protein synthesis

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16
Q

How are polypetides able to fold into complex and unique structures?

A

The R groups on the amino acids are able to form bonds which fold the polypeptide chains. The different sequence of R groups make the chains fold in unique ways.

17
Q

What is the definition of the primary structure of proteins?

A

It is the sequence in which the amino acids are joined

18
Q

What is the definition of the secondary structure of proteins?

A

It is the formation of hydrogen bonds within the amino acid chain

19
Q

What are the two ways in which the formation of hydrogen bonds can alter the shape of the amino acid chain?

A

The hydrogen bonds may create a alpha helix type structure Or the hydrogen bonds may form between parallel polypeptide chains which would create a beta pleated sheet structure.

20
Q

What is the definition of the tertiary structure of proteins?

A

It is when the R groups interact with each other to enable further folding of the polypeptide chain.

21
Q

What are the 4 interactions that could occur between the R groups?

A

Hydrophobic and hydrophilic interactions Hydrogen bonds Ionic bonds Disulfide bonds (also known as disulfide bridges)

22
Q

What are Hydrophobic and hydrophilic interactions?

A

They are weak interaction between polar and non-polar R groups

23
Q

What are Hydrogen bonds?

A

They ate the weakest of the bonds formed and they are between the delta charges

24
Q

What are Ionic bonds?

A

These are stronger than hydrogen bonds and form between oppositely charged R-groups

25
Q

What are Disulfide bonds (also known as disulfide bridges)?

A

These are covalent and so the strongest of all the bonds. However, they only occur between R-groups that contain sulfur atoms

26
Q

What is the definition of the Quaternary structure of proteins?

A

It is the interaction between two or more identical or different protein chains (as opposed to within one protein chain). The interactions between the sub-units are the same in tertiary structure.

27
Q

How are peptides broken back into their individual amino acids?

A

A water molecule is added to break the peptide bond in a hydrolysis reaction. A enzyme named protease catalyses the reaction.