AA, proteins and DNA Flashcards

1
Q

functional groups of AA

A

NH2 and COOH

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2
Q

how many naturally occurring AA are there in the body

A

20

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3
Q

what type of AA are found in the body

A

alpha

the NH2 is always on the carbon next to COOH

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4
Q

generic formula for an alpha AA

A
R
            I
H2N - C - COOH
            I
            H
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5
Q

which enantiomer do alpha AA exist as in nature

A
  • enantiomer
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6
Q

is the product from AA being synthesises naturally optically active

A

no

a racemix is formed as the CN- can attack from above or below the planar C=O

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7
Q

in what form do AA exist as solids

A

zwitterions

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8
Q

what colour are zwitterions

A

white solids

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9
Q

zwitterion

A

ions which have both a permanent positive and negative charge but are neutral overall

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10
Q

zwitterion AA

A
R
              I
H3N+ - C - COO- 
              I
              H
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11
Q

what happens to AA in acidic conditions

A

gains a proton on NH2 group

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12
Q

what happens to AA in alkaline conditions

A

loses a proton from COOH group

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13
Q

peptide linkage

A

CONH

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14
Q

what name is given to chains of AA up to 50 AA

A

polypeptide

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15
Q

what name is given to a chain of AA with more than 50

A

proteins

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16
Q

conditions needed for hydrolysis to occur

A

6 mol dm3
HCl
reflux for 24 hours

17
Q

primary structure

A

sequence of AA along the protein chain bonded by covalent bonds

18
Q

secondary structure

A

shape of the protein chain

19
Q

how is the secondary structure held together

A

hydrogen bonding

20
Q

tertiary shape of a protein

A

alpha helix or beta pleated sheet is folded into a complex 3D shape

21
Q

how is the tertiary structure held together

A

hydrogen bonding
ionic interactions
disulphide bridges
van der waals

22
Q

what is TLC plate made of

A

plastic sheet coated with silica

this is the stationary phase

23
Q

describe the process of TLC

A

spot the samples onto a pencil line a few cm above the base
place this in a beaker with solvent lower than the pencil line
wait until the solvent front is almost at the top of the plate
remove and analyse

24
Q

how do you calculate the Rf value

A

distance moved by that substance divided by the distance moved by the solvent front

25
Q

what is 2D TLC

A

uses a square TLC plate
spot the AA in one corner then run TLC in first solvent
flip the plate through 90’ and repeat TLC in a second different solvent

26
Q

what is an enzyme

A

protein based catalyst that speed up reactions in the body by factors of up to 10^10

27
Q

structure of an enzyme

A

globular protein with a creft/crevice in it, known as an active site

28
Q

how structure help the function

A

the reacting molecules fit precisely into the active site and are held at exactly the right orientation to react

29
Q

enzymes increase the ror

A

reacting molecules form temporary bonds to the enzyme

this weakens the bonds in the molecules promotes electron movement and lowers Ea

30
Q

what does the stereospecificity of enzymes mean

A

active sites are so selective of the shape of substrates that only reactions involving one enantiomer are catalysed

31
Q

example of a drug that works through enzyme inhibition

A

penicillin

32
Q

DNA

A

deoxyribonucleic acid

33
Q

what does DNA do

A

present in all cells and is a blueprint from which all organisms are made

34
Q

cisplatin

A

Cl NH3
Pt
Cl NH3

35
Q

function of cisplatin

A

bonds to strands of DNA to distort shape and prevent cell replication
bonds to N atoms on 2 adjacent G bases
N atom replaces Cl- ligand