Biochemistry - Amino Acids Flashcards

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1
Q

Alpha Amino Acids

A

These are AA with primary amino grup(NH2)

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2
Q

What does pK value measure?

A

Availability of protons, the lower the less tightly they are held.

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3
Q

What are features of Amino Acids?

A

R Group
Dipolar due to Amino and Carboxylic functional groups readily ionising.

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4
Q

Conjugate

A

This is a substance formed when an acid loses a hydrogen ion

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5
Q

Zwitterions

A

Neutral molecules that intramolecularly have both a positve and negative charge

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6
Q

Why is all AA being zwitterions important?

A

More soluble in polar solvents than nonpolar

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7
Q

Where are peptide bonds found?

A

Between CO and NH by condensation reactions

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8
Q

Condensation Reactions

A

These are reactions between two reactangs yielding one large product and a smaller product such as water.

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9
Q

What is the primary structure of protein?

A

Linear peptide with NTD and CTD with variable electrostatic charges

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10
Q

What are the three categories of electrostatic charge of amino side chains?

A

Polar, Charged or Non Polar

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11
Q

Non Polar AA

A

Nine, like glycine with H and Ala, Val, Leu being aliphatic

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12
Q

Aliphatic

A

These are organic compounds where the carbon atoms form open chains.

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13
Q

What is the side chain of methionine?

A

Thioether side chain

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14
Q

Uncharged Polar Side Chains

A

These have either Hydroxyl, Amide or Thiol groups

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15
Q

Serine

A

This has a thiol group with capacity of disulphide bond formation

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16
Q

Amide

A

This is a functional group containg a carbonyl group and a nitrogen atom

17
Q

Thiol(Sulfhydryl)

A

These consist of a S with two lone pairs bound to a H

18
Q

Charged Polar Side Chaines

A

These are either anionic or cationinc, being 5

19
Q

How is histidine unique?

A

Carrying an imidazole group ionizing readily at physiological pH so can be both neutral or cationic

20
Q

What do polypeptide chains depend on?

A

Hydration tendency of polar and ionic side chains and non-polar side chains with each other.

21
Q

Hydrophobic Effect

A

THis is the tendency of non-polar molecules and molecular segments in an aqueous solution to avoid contact with water molecules

22
Q

Which amino acids are optically active?

A

All except glycine

23
Q

Optically Active

A

This is the ability of a substance to rotate the plane of polarization of a bean that passes through it.

24
Q

Why are AA optically active?

A

Chiral Centre

25
Q

Chiral Centre

A

This is an atom in a molecule bounded to four different chemical species.

26
Q

Enantiomer

A

Two isomers that cannot be superimposed on one another.

27
Q

Why is chirality important?

A

It derives enantiomer forms.

28
Q

Superimposition

A

This is where you may lay two things over one another where you cant tell them apart

29
Q

What are the two Enantiomers of amino acids?

A

Can exist in L and D forms being mirror images.

30
Q

Plane-polarized light

A

This is the light form in which the electric field oscillates in a single plane.

31
Q

How does Plane-Polarised Light relate to AA?

A

Light passing through chiral molecules results in CW or CCW optical rotation

32
Q

Why does AA rotate under plane-polarised light?

A

Asymmetric arrangement of atoms, where EM radiation interact with electrons, inducing oscillations creating polarized EM field rotation in direction of light propogation

33
Q

What is an example of different biological functions in AA enantiomers?

A

Thalidomide L forms for sedation whilst D forms birth defects

34
Q

Fischer Projection

A

This is a 2D representation of a 3D organic molecule

35
Q

Racemic Mixture

A

This means equal amounts of each enantiomer

36
Q

How is equilibrium favoured in one direction in racemic mixtures?

A

Chiral processes like enzyme.