Proteins ๐Ÿ’ช๐Ÿฝ Flashcards

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1
Q

Describe the sub sections that make up a protein.

A

Monomer โ€”> amino acid.

Dipeptide โ€”-> two amino acids.

Polypeptide โ€”-> more than two amino acids.

Protein โ€”-> one or more polypeptide.

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2
Q

What is the chemical composition of an amino acid

A

Contains a central carbon.
Has two groups, an amino group and a carboxyl group.
Contains an R group which is a variable region where the amino acid changes from another and gives the amino acid its properties.

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3
Q

What is the second level of protein structure?

A

Secondary structure

chain starts to coil in sectionsโ€”-> alpha helix
other sections fold into each other โ€”โ€”> beta pleated sheets

This is due to the hydrogen bonds between the amino group of one amino acid and the carboxyl group of another.

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3
Q

What happens when two amino acids join together?

A

Through a condensation reaction.
Hydrogen from the amino group and hydroxyl from the carboxyl group react together.
Form a peptide bond.
Loss of water.

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3
Q

What is the first level of protein structure?

A

Primary structure

initial polypeptide chain held together by peptide bonds.

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4
Q

What is the third level of protein structure?

A

Tertiary structure

More bonds start to form between different parts of the polypeptide chains.
Determines 3D shape of protein.
Done through the interaction of the amino acid R group as different R groups have different properties.
Can form hydrogen bonds/ ionic bonds.
Disulphide bonds are the strongest bonds and formed when two cysteine bonds interact.

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5
Q

What is the fourth level of protein structure?

A

Interactions between two or more polypeptide chains.

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6
Q

What are globular proteins?

A

Round/spherical, complex, 3D shapes which are water soluble because they have a hydrophilic R group on the surface of the protein to interact with water molecules.

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7
Q

Describe haemoglobin.

A

Made from 4 polypeptide subunits (2 alpha and 2 beta).
Function is to bind reversibly to oxygen to transport them to body tissues.
Each subunit contain the prosthetic group haem (conjugated protein).
Contains Fe2+ which binds to the oxygen.
Quaternary structure changes slightly to carry more oxygen.

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8
Q

Describe insulin

A

Globular protein which has 2 polypeptide bonds.
Held together by disulphide bonds.
Needed for the regulation of blood glucose concentrations.

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9
Q

Describe amylase.

A

Globular protein which catalyses the breakdown off starch.
Present in saliva.
Has single polypeptide chain.

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10
Q

Describe catalase.

A

Enzyme that catalyses the decomposition of hydrogen peroxide to water and oxygen.
Quaternary structure with four prosthetic haem groups. (Fe2+)

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11
Q

What is a fibrous protein?

A

Strong rod shaped protein, insoluble non complex 3D shape.
Structural roles in bones and tendons.

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12
Q

What is a conjugated protein?

A

Globular portion with a prosthetic group (non protein component)

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13
Q

Describe collagen.

A

Made by 3 polypeptide chains wound together to form a triple helix.
Large number of H-bonds form between polypeptide chains.
Stabilises quaternary structure of proteins and has strong cross links.

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14
Q

Describe keratin.

A

Fibrous protein found in external animal structures like hair and nails.
Made of cysteine and disulphide bridges provide extra strength.
Strong covalent bonds.

15
Q

Describe elastin.

A

Found in elastic muscles tissues like the wall of arteries.
Can return back to shape after being stretched.
Has hydrophobic regions.