Lecture 4 - building blocks of proteins Flashcards

1
Q

are amino acids usually found in the L or D form in biological systems

A

L form

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2
Q

are amino acids chiral

A

yes

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3
Q

what is a zwitterion

A

when they have both a positive and negative charge

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4
Q

are non polar side chains hydrophobic or hydrophilic

A

hydrophobic

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5
Q

how to tell if the amino acid is non polar

A

if it has only C or H at the end of their side chain

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6
Q

how to tell if the amino acid is polar

A

if it also has -OH, -NH2 or -O in their side chain
if it is able to form bonds with other atoms

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7
Q

are polar amino acids hydrophilic or hydrophobic

A

hydrophilic

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8
Q

how to know if a amino acid is positively charged polar

A

same as polar but has + charge at pH 7

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9
Q

how to know if a amino acid is negatively charged polar

A

same as polar but has - charge at pH 7

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10
Q

how to know if something is ionisable or not

A
  • its polar
  • has an H atom that can participate in acid base reactions
  • donates and accepts electrons
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11
Q

what does the pKa of an ionisable group on amino acid or protein equal

A

the pH at which the group is 50% ionised

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12
Q

what does the pI or isoelectric point equal

A

the pH at which the net charge on an amino acid or protein is zero

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13
Q

what is post translational modification

A

a chemical group can be added to an amino acid residue AFTER translation has occurred

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14
Q

what happens due to post translational modification

A

the protein is modified which can switch it on or off

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15
Q

what amino acid is different to the others in terms of post translational modification

A

cystine = forms a disulfide bond instead of adding something

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16
Q

what type of bond is a peptide bond

A

a covalent bond

17
Q

what are other features of a peptide bond that are important for preventing steric hinderance

A

planar = flat
trans = a-carbons go on opposite sides
dipole = ends have opposite charges

18
Q

what is special about the peptide bond in terms of the double bond

A

it has partial double bond character (when the double bond can switch from the O to the N ?)

19
Q

what do amino acids have

A

An alpha carbon, amino group, carboxyl group and side chain (R)

20
Q

what are enantiomers

A

non superimposable mirror images

21
Q

what is cystine commonly found in

A

proteases

22
Q

what is glycines R group

A

A hydrogen making it non-chiral, flexible because its R group is small meaning it is found in regions which need to get tight and close together

23
Q

What does the R group in proline do?

A

Bends back to the main chain N forming a 5 membered covalently closed ring. This makes it rigid and an imino acid rather than an amino acid as it contains an amine

24
Q

How are negatively charged polar (acidic) amino acids shown?

A

As the conjugate base where the protons are already donated

25
Q

how is the peptide bond formed

A

via dehydration between C-terminal of one amino acid and N-terminal of another

26
Q

what is a peptide

A

short stretch of amino acids joined by peptide bonds

27
Q

what is a polypeptide

A

a longer stretch of amino acids joined by peptide bonds

28
Q

what is a protein

A

longer chain of amino acids, usually with a biological function

29
Q

what is an amino acid residue

A

amino acids that are covalently joined together in peptide of a protein

30
Q

When will disulphide bonds form?

A

In an oxidising environment

31
Q

When will disulphide bonds break?

A

In a reducing environment

32
Q

what are types of post translational modification

A

Phosphorylation, hydroxylation, carboxylation, metal ending, iodination, glycosylation and many others