AA, proteins and DNA Flashcards

(35 cards)

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
what is 2D TLC
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
what is an enzyme
protein based catalyst that speed up reactions in the body by factors of up to 10^10
27
structure of an enzyme
globular protein with a creft/crevice in it, known as an active site
28
how structure help the function
the reacting molecules fit precisely into the active site and are held at exactly the right orientation to react
29
enzymes increase the ror
reacting molecules form temporary bonds to the enzyme | this weakens the bonds in the molecules promotes electron movement and lowers Ea
30
what does the stereospecificity of enzymes mean
active sites are so selective of the shape of substrates that only reactions involving one enantiomer are catalysed
31
example of a drug that works through enzyme inhibition
penicillin
32
DNA
deoxyribonucleic acid
33
what does DNA do
present in all cells and is a blueprint from which all organisms are made
34
cisplatin
Cl NH3 Pt Cl NH3
35
function of cisplatin
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