Protein Structure And Function Flashcards

1
Q

What are the General function of proteins?

A
  • carrier
  • metabolic
  • part of cellular machinery
  • sensing molecules
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2
Q

Give the structure of an Amino acid in space

A

Tetrahedral arrangement of atoms with carbon at the centre.

R chain makes the specific physiochemical properties

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3
Q

Give the forms of Ionised amino acids

A

NH2-> NH3+
COOH->COO-

Can also be a zwitter ion (double ion) when both happen so its polar but also neutral as charges cancel out

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4
Q

How many isomers of each amino acid and which is the exception?

A

2 as you have both D (dextro) and L (Levo) isomers

Glycine as the R group is Hydrogen

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5
Q

How to remember difference between L and D amino acid structures

A

L - groups read CORN in the clockwise direction

D- groups read CORN in the anticlockwise direction

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6
Q

Which form of amino acid is found in living organisms and what does the other do?

A

L form is in living organisms

D form in bacterial cell walls and in some therapeutics

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7
Q

What is a peptide residue?

A

A repeated unit or polypeptide chain.
Consists of the α carbon, C=O and NH group
Almost always trans

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8
Q

Describe Secondary proteins

A

Hydrogen bonding between different parts of the same chain- causes either β sheets, α helixes or β turns

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9
Q

give the structure of β sheets

A

Can be either antiparallel or parallel

In parallel the loops (turns) linking the strands go over the rest of the chain and they don’t in antiparallel

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10
Q

what is an α helix structure?

A

Right handed helix, stabilised by hydrogen bonds

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11
Q

How many residues between each H bond in the α helix?

A

4 residues (on the 1st and 5th residue)

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12
Q

Why is the orientation of side chains in α helixes important?

A

It gives the proteins their properties as they protrude out from the structure

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13
Q

Give the structure of Tertiary and quaternary proteins

A

Generally globular

Depends on interaction between side chains

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14
Q

How are tertiary and quaternary protein structures held together?

A

Lots of weak chemical bonds but may also be stabilised by covalent bonds

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15
Q

How is the quaternary protein structure different to the tertiary protein structure

A

In quaternary the bonds are between different polypeptide chains, but in tertiary the bonds are between the same chain

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16
Q

What is a cofactor?

A

Other extra molecules for their function or folding

17
Q

Which structures are cofactors found in?

A

Both tertiary and quaternary proteins

18
Q

What shape are water soluable proteins and where are the hydrophilic residues?

A

Generally globular but can sometimes be in filaments or tubes. Hydrophilic residues are on the outside

19
Q

Where are the hydrophilic residues in non-aqueous environments and why?

A

On the inside- this allows it to interact with the lipid membranes