Proteins 1+2 Flashcards

1
Q

What are amino acids?

What three groups can they be divided into?

A

Amino acids are the building blocks of proteins.

Non-essential: the body is able to produce them.
Conditionally essential: supplemented in the diet for young or compromised animals.
Essential: the body is unable to produce them and they need to be acquired in the diet.

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2
Q

Give examples of non-essential amino acids.

A

Alanine, asparagine, aspartate, glutamate and serine.

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3
Q

Give examples of conditionally essential amino acids.

A

Arginine, cysteine, glutamine, glycine, proline, and tyrosine.

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4
Q

Give examples of essential amino acids.

A

Histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine.

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5
Q

What structure do amino acids have?

A

They have a central carbon atom, bound with a carboxyl group, a hydrogen atom, an amino group and a variable side chain.
Amino acids can also act as acids and bases.

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6
Q

How many structure levels do proteins have and what are they called?

A

4.

Primary, secondary, tertiary, and sometimes quaternary.

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7
Q

What is the function of the primary structure?

A

The primary sequence of a protein determines its 3D conformation and function.
Changes in the amino acid sequence can severely compromise the ability of the protein to carry out its function.

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8
Q

What is a peptide bond?

A

This bond is when the carboxyl group of one amino acid reacts with the amino group of another amino acid, forming a peptide bond.

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9
Q

What is the function of the secondary structure?

A

The secondary structure of a protein describes the local special arrangement of amino acids.

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10
Q

What is the function of the tertiary structure?

A

This tier describes the overall 3D conformation of the polypeptide chain. Includes how elements of the secondary structures pack together and how R groups interact.

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11
Q

What are three methods of arrangements?

A

Reversible attractions/repulsions.
Hydrogen bonds.
Hydrophobic & hydrophilic regions form from arrangements from non-polar & polar R groups.

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12
Q

Name three examples of globular proteins.

A

Enzymes, transport proteins, motor proteins, regulatory proteins & immunoglobulins.

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13
Q

What are globular proteins?

A

Different segments of the polypeptide chain fold back on each other, generating a more compact shape than is seen with the fibrous proteins.

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14
Q

What is the function of the quaternary structure?

A

This tier describes the 3D arrangement of subunits in a multi-subunit protein, resulting from specific interactions between the subunits.

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15
Q

What else can amino acids make?

A

They can make non-protein biomolecules.

For example, hormones, porphyrins, antibiotics, pigments, neurotransmitters, nucleotides & alkaloids.

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16
Q

What are porphyrins?

A

Formed from glycine.
Water soluble, nitrogenous pigments.
Have a cylindrical structure.
Most well-known one is haem.

17
Q

What is haem?

A

A cofactor of haemoglobin and a source of bile pigments.
It releases iron ions when degraded.
It is converted into biliverdin, then bilirubin - a visible colour change.

18
Q

What are three methods of protein testing?

A

Colorimetric assays.
SDS-PAGE & Western blotting.
Enzyme Linked Immunosorbent Assays (ELISA).

19
Q

What are colorimetric assays?

A

These are reactions that use a colour change to infer protein presence or activity.
A semi-quantitative measure.
Uses bromophenol blue & other compounds.

20
Q

What is SDS-PAGE & Western blotting?

A

Sodium dodecyl sulphate (SDS) polyacrylamide gel electrophoresis (PAGE) separates proteins according to size.

21
Q

How does SDS-PAGE & Western blotting work?

A

The gel has pores which trap proteins; big proteins are less able to pass.
An electrical current is applied across the gel & the proteins follow the current.
Once separated, the proteins are transferred to a thin membrane.
Detected using antibodies.

22
Q

How do Enzyme Linked Immunosorbent Assays (ELISA) work?

A

Cells are fixed with a fixature like acetone or methanol.
Primary antibody is added & allowed to bind to the protein of interest.
The labelled secondary antibody is then added to bind the primary.
The secondary antibody is bound to a fluorescent marker.
This technique is useful when you need to know protein location over quantity.

23
Q

What are enzymes?

A

Biological catalysts.
They alter the rate of reactions without taking part in them.
Enzymes have active sites that are where the catalytic reactions occur.

24
Q

What are coenzymes?

A

Coenzymes act as carriers and donors of functional groups.