Lecture 4- Protein Strucutre Flashcards

1
Q

What is a zwitterion

A

It is the ionised form of an amino acid. The form found in the body nh3+ and coo-

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2
Q

What is an amino acid residue?

A

Part of amino acid left after it has been joined by a peptide bond to form a protein.

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3
Q

If pka is 9 but PH is 7.4 will amino acid be protonated or deprotonated

A

Protonated as ph is Lowe will be more H+ and so it will take a proton.

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4
Q

What way are peptide bonds?

A

Planer and rigid due to partial double bond characteristics

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5
Q

How do you tell if a peptide is trans or cis?

A

Trans if R groups opposit cis if they’re on the same side.

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6
Q

What is the PI or isoelectric point of a protein?

A

It is the pH at which there is no net charge on the protein. For acidic proteins it will be less than 7 etc. It can be found by averaging the pka’s of the amino acid residues.

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7
Q

What is pka of an amino acid?

A

Measure of the likelihood of the amino acid to be ionised.

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8
Q

What is a conjugated protein?

A

One that has a covalently linked chemical compound in addition to the amino acids. Eg the heme or iron porphyrin ring in haemoglobin

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9
Q

What holds primary structure together?

A

Covalent bonds

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10
Q

What hold secondary structure together?

A

Hydrogen bonds

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11
Q

What is tertiary structure?

A

Spatial arrangement of amino acids far apart in the protein sequence

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12
Q

What is secondary structure

A

The linear amino acid sequence and how they interact with each other.

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13
Q

What is interesting about secreted proteins?

A

They tend to have more covalent bonds to hold them together in an unstable environment.

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14
Q

What type of bonding do you get in tertiary protein structure?

A

Generally non-covalent but can be anything
A lot of disulphides bonds as with quarternarmy structure

Also get hydrogen bonds, van der walls, hydrophobic interactions and ionic bonds

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15
Q

Do you know polarities etc of amino acids? Be able to recognise them?

A

Yes or no

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16
Q

Can you use the Henderson hasselbach equation?

A

Example in workbook

17
Q

How does pH denature proteins

A

It alters ionisation state of amino acids

18
Q

What are the proteins that aid folding called?

A

Chaperones

19
Q

What is the danger of a misfolded proteins?

A

It encourages other proteins to also missfold. Amyloid fibres are an example

20
Q

How do proteins fold?

A

In many steps. Localised folding occurs at each step and stable conformations are maintained. This is driven by the need to find the most stable conformation.