Proteins Flashcards

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1
Q

Amino Acid

A

A monomer that will join with other amino acids to form a protein

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2
Q

Dipeptide

A

Two amino acids bonded together via a peptide bond

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3
Q

Polypeptide

A

Many amino acids bonded together via peptide bonds

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4
Q

Protein

A

A combination of polypeptides

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5
Q

Amine Group

A

-NH2, a basic group where the amino part of amino acid comes from

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6
Q

Carboxyl Group

A

-COOH, an acidic group where the acid part of amino acid comes from

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7
Q

R Group

A

A side group that can be comprised of different chemical groups

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8
Q

Secondary Structure

A

The arrangement of the primary structure when considering hydrogen bonds.

This forms either an alpha helix or a beta pleated sheet

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9
Q

Alpha Helix

A

A helix shape that can be formed when considering a polypeptide’s secondary structure

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10
Q

Beta Pleated Sheet

A

A bent v-shaped structure that can be formed when considering a polypeptide’s secondary structure

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11
Q

Tertiary Structure

A

The overall 3D shape of the polypeptide chain, considering all types of bonds; hydrogen bonds, ionic bonds and disulphide bridges. This results in a compact structure

Has hydrophobic interactions between non polar sections.

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12
Q

Quarternary Structure

A

The 3D shape of multiple polypeptide chains combined into one complex molecule. This also considers external associated non-proteins

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13
Q

Prosthetic Groups

A

Associated non-proteins which affect the quarternary structure of a protein

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14
Q

Process of the Biuret Test

A

Add 2cm^3 of the sample with an equal volume of sodium hydroxide.

Add a few drops of very dilute copper(II) sulphate (0.05%) and mix.

A positive test turns purple, a negative test remains blue.

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15
Q

Fibrous Proteins

A

Serve a structural function

Support and protect tissues such as collagen

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16
Q

Globular Proteins

A

Carry out a metabolic function

(enzymes, antibodies, transport proteins)

Spherical & Tightly folded

17
Q

Primary Structure of Collagen

A

An unbranched polypeptide chain

18
Q

Secondary Structure of Collagen

A

Very tightly wound, an alpha helix

19
Q

Tertiary Structure of Collagen

A

Winds into another large helix

20
Q

Quarternary Structure of Collagen

A

Made up of three polypeptide chains with the same tertiary structure, wound together in a rope shape

21
Q

Uses of Collagen

A

Fibrous protein

In hair, as part of tendons

22
Q

What can break ionic bonds?

A

Change in pH

23
Q

What are disulfide bonds between?

A

Cysteine amino acids

24
Q

Competitive Inhibitors

A

Compete with substrate for active site

Have a SIMILAR shape as substrate

Blocks the active site so no reaction can take place

Inhibitor is not permanently bound to active site

The greater the concentration of inhibitor the slower the rate of reaction

25
Q

Non Competitive Inhibitors

A

Bind to the enzyme AWAY from its active site

This causes the active site to change shape

Substrate molecule cannot bind

Enzyme cannot function

26
Q

What is the primary structure of a polypeptide?

A

Sequence of amino acids

27
Q

Examples of proteins with quarternary structure.

A

Haemoglobin

Antibodies