Chapter 5: Proteins, Structure, And Synthesis Flashcards

1
Q

What is a protein?

A

A macromolecule in biological systems made up of a combination of the 20 different amino acids. They are essential in several cellular tasks in the body.

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2
Q

What are the two main types of protein and what are their roles?

A

Enzymes: proteins that catalyse and control metabolic reactions.
Transporters: proteins that transport molecules through otherwise impermeable membranes.

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3
Q

What reaction links two amino acids?

A

Condensation reaction

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4
Q

Describe the structure of an amino acid and how it condenses to an amino acid chain

A

Left: amino acids as non-ionised, separate molecules
Right: amino acids as ionised chain

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5
Q

Are amino acids connected to each other rigidly (can movement occur)?

A

No, the central carbon in each amino acid is a point of rotation so the orientation of them can be defined by dedihedral angles.

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6
Q

Describe the primary structure of a protein

A

The initial form of a protein; a singular polypeptide chain made up of a series of amino acids. This structure determines the ultimate shape, hence function, of the protein.

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7
Q

Describe the secondary structure of a protein

A

‘Folding’ of the the primary structure into local motifs, the α-helix and the β-sheet. The number, types of and extent of these motifs determines the secondary structure.

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8
Q

What determines if the secondary structure is an α-helix or β-sheet?

A

The characteristic set of dihedral angles for the peptide bond of the molecules.

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9
Q

What bond forms the α-helix and the β-sheet?

A

Hydrogen bonds between the -NH group and -C=O group (but in different places).

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10
Q

Where do bonds form to produce an α-helix?

A

Between the two helical pitches.

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11
Q

Where do bonds form to produce a β-sheet?

A

Between parallel strands of amino acids.

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12
Q

Describe the tertiary structure of a protein

A

Further ‘twisting’ of secondary structure proteins into more complex shapes meaning that they have a 3D globular configuration.

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13
Q

Give 3 examples of bonds that maintain the tertiary structure

A
  • Disulphide bridges
  • Ionic bonds
  • Hydrogen bonds
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14
Q

Describe the quaternary structure of a protein

A

The subunits of a molecular complex. Multiple quaternary structure proteins are combined together with non-protein prosthetic groups to produce large structures e.g. haemoglobin.

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15
Q

Define the Ramachandran plot

A

A plot of the dihedral angle combination, φ and ψ, for all the peptide bonds in a protein. The density of these plots determines how many α-helices and β-sheets there are in a protein.

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16
Q

What are the dihedral angles for an α-helix?

A

For an α-helix: φ = -57º; ψ = -47º

17
Q

What are the dihedral angles for a β-sheet?

A

For a β-sheet: φ = -100º; ψ = 140º

18
Q

What are the 6 important interactions that can impact a proteins structure?

A

• Disulphide bonds between cysteine (amino acid) residues in polypeptides.
• Covalent bonds between two sulphur atoms.
• Electrostatic interactions, known as salt bridges, between the charge residue of two amino acids.
• Cation π interactions between the amino acids tryptophan, arginine, and/or lysine.
• Hydrophobic interactions are mainly responsible for initial protein folding.
• Hydrogen bonds provide stabilisation.

19
Q

What percentage of chemical groups form hydrogen bonds in proteins given that they are able to? (EXTRA: what is the result of this?)

A

90%

EXTRA: even though the bond is weak, in large numbers the overall impact is great.

20
Q

What are the two stages of protein synthesis?

A

Transcription and translation.

21
Q

Where is translation performed?

A

In the ribosome (found in the cytoplasm of a cell).

22
Q

What is a ribosome?

A

A complex catalytic molecule consisting of over 50 proteins and several rRNA, ribosomal RNA, molecules. These components form two subunits in the ribosome. There are 10 ribosomes in the typical cell.