Proteins Flashcards

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1
Q

What four groups are attached to the central carbon of an amino acid?

A

NH2, COOH, H and variable component R

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2
Q

What are the four classes of amino acids?

A

acidic, basic, polar and non-polar

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3
Q

Which part of the amino acid decides which class the amino acid belongs to?

A

The R group

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4
Q

Which class of R group gives a hydrophobic reaction with water?

A

Non-polar

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5
Q

Give examples of Proteins which are, acidic, basic, polar and non-polar, and the functional group which causes this.

A

Acidic: aspartic acid COOH
Basic: Lysine, NH2
Polar: Serine OH
Non-polar: Alanine CH3

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6
Q

When are amino acids linked together?

A

During translation of mRNA at the ribosome

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7
Q

What type of reaction is the formation of a peptide bond?

A

Condensation reaction caused by an enzyme.

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8
Q

What is the the primary structure of a protein?

A

The sequence of amino acids that make up a polypeptide chain.

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9
Q

What are the two ends of a polypeptide chain known as?

A

N terminus and a C terminus

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10
Q

What is the secondary structure of a protein stabilised by?

A

Hydrogen bonds between the atoms of different peptide bonds in the chain.

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11
Q

Which part of the polypeptide with a slight negative and positive charge?

A

Positive: The hydrogen of the NH2 group.
Negative: Oxygen of the COOH

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12
Q

What are the two type of secondary structure

A

Alpha Helix and Beta Sheet

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13
Q

Describe the structure of an alpha helix

A

A spiral with the R groups sticking outwards

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14
Q

What is the structure of a Beta sheet

A

Parts of polypeptide chain running alongside each other forming a corrugated sheet, with the R groups sitting above and below.

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15
Q

What does an anti-parallel and parallel chain consist of?

A

anti-parallel: Chains in opposite directions with respect to NC polarity
parallel: Chains in the same direction with respect to NC polarity.

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16
Q

What is the tertiary shape of a protein?

A

The 3-dimensional shape of a protein

17
Q

What is the tertiary shape of a protein stabilised by?

A

Interactions between R groups of amino acids

18
Q

Why are the R groups close together in the tertiary structure?

A

Because of the folding in the secondary structure

19
Q

Name five types of interactions between R groups

A
Hydrophobic interactions
Van der Waals interactions
Hydrogen bonding
Ionic bonds
Disulphide bridges
20
Q

Describe hydrophobic interactions

A

Non polar R groups are usually found on the inside of the protein. Other R groups are usually found on the outside.

21
Q

Describe van der waals interactions

A

Very weak attractions between the electron clouds of atoms

22
Q

Describe hydrogen bonding

A

The weak negative charge of oxygen on C=O is attracted to the weak positive charge of the hydrogen on an OH or NH2 group.

23
Q

Describe ionic bonds

A

The COOH and NH2 groups ionise to become COOH- and NH3+. These groups are strongly charged and can attract one another

24
Q

Describe disulphide bridges

A

Covalent bonds form due to reactions between the sulphur-containing R groups of cysteines.

25
Q

What is the name given to the non-protein groups that are incorporated into the polypeptide chain in the tertiary structure

A

Prosthetic groups

26
Q

What does the quaternary structure of a protein consist of?

A

Different polypeptide sub-units linked by R group interactions