Proteins and Amino acids Flashcards

(80 cards)

1
Q

Proteins are made up of which monomers

A

Amino acids

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2
Q

How is it suggested that eukayotes and Archaea are linked
Why wasnt always believed

A

It is believed that eukaryotes came from archaea
This wasn’t always believed due to the similarities in appears from bacteria and archaea, where archaea was believed to be a form of bacteria
Now in research we can use the molecular biology of archaea to make informed decisions about human cells

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3
Q

Why is it belived that viruses could be living

A

The mimivirus, which was discovered was thought to be a bacterium but was actually a virus which is alive

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4
Q

Protein take up what % of of macromolecules in a cell

A

15%
This is the vast marority compared to other macromolecules

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5
Q

You can describe cells as

A

Highly organised
Even prokaryotes without a nucleus

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6
Q

All naturally occuring proteins are based upon which type of amino acids

A

L-amino acids

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7
Q

What type of reaction is it which forms a peptide bond between the two amino acids
What is the name of the reverse of this reaction

A

Condensation
Hydrolysis

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8
Q

How many common, naturally occuring amino acids

A

20

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9
Q

Which amino acid is Ala
What is its one letter abbrebiation

A

Alanine
A

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10
Q

Which amino acid is Arg
What is its one letter abbrebiation

A

Arginine
R

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11
Q

Which amino acid is Asn
What is its one letter abbrebiation

A

Asparagine
N

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12
Q

Which amino acid is Asp
What is its one letter abbrebiation

A

Aspartic acid
D

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13
Q

Which amino acid is Cys
What is its one letter abbrebiation

A

Cysteine
C

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14
Q

Which amino acid is Glu
What is its one letter abbrebiation

A

Glycine
G

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15
Q

Which amino acid is His
What is its one letter abbrebiation

A

Histidine
H

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16
Q

Which amino acid is ile
What is its one letter abbrebiation

A

Isoleucine
i

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17
Q

Which amino acid is Leu
What is its one letter abbrebiation

A

Leucine
L

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18
Q

Which amino acid is Lys
What is its one letter abbrebiation

A

Lysine
K

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19
Q

Which amino acid is Met
What is its one letter abbrebiation

A

Methionine
M

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20
Q

Which amino acid is Phe
What is its one letter abbrebiation

A

Phenylalanine
F

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21
Q

Which amino acid is Pro
What is its one letter abbrebiation

A

Proline
P

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22
Q

Which amino acid is Ser
What is its one letter abbrebiation

A

Serine
S

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23
Q

Which amino acid is Thr
What is its one letter abbrebiation

A

Threonine
T

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24
Q

Which amino acid is Trp
What is its one letter abbrebiation

A

Tryptophan
W

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25
Which amino acid is Tyr What is its one letter abbrebiation
Tyrosine Y
26
Which amino acid is Val What is its one letter abbrebiation
Valine V
27
What group on the amino acids affects its chemical properties
The R group
28
Which amino acid R group is this?
Alanine
29
Which amino acid R group is this?
Arginine
30
Which amino acid R group is this?
Asparagine
31
Which amino acid R group is this?
Aspartic acid
32
Which amino acid R group is this?
Cysteine
33
Which amino acid R group is this?
Glutamic acid
34
Which amino acid R group is this?
Glutamine
35
Which amino acid R group is this?
Glycine
36
Which amino acid R group is this?
histidine
37
Which amino acid R group is this?
Isoleucine
38
Which amino acid R group is this?
Leucine
39
Which amino acid R group is this?
Lysine
40
Which amino acid R group is this?
Methionine
41
Which amino acid R group is this?
Phenylalanine
42
Which amino acid R group is this?
Proline
43
Which amino acid R group is this?
Serine
44
Which amino acid R group is this?
Threonine
45
Which amino acid R group is this?
Tryptophan
46
Which amino acid R group is this?
Tryonsine
47
Which amino acid R group is this?
Valine
48
How many amino acids can be made in cells, and how many much come from the diet of the 20 nautrally occuring amino acids
11 of the core 20 are made in cells 9 amino acids cannot be synthesied in humans
49
What is the general structure of an amino acids (except proline)
Alpha carbon: chrial in all amino acids (except glycine) Carboxyl group Amine group R-group
50
Amino acids (bar glycine) are chiral What does this mean
They have 4 different groups bonded to the central carbon This means they can form enantiomers in space
51
What are the two enantiomers of Alanine
L-Alanine and D-Alanine
52
Amino acids in proteins are always which isomer
L-isomers They are homochiral
53
What does Aliphatic mean
Means the R-group chain is not branched
54
What does Aromatic mean
the R-group is based on a benzene ring (hydrophobic)
55
What does polar mean
the R group carries a small charge, both positive and negative
56
What does charged mean
the R-group is ionisable creating +ve or -ve charge depending on pH and type of R group (electrostatic/ionic interactions)
57
Which amino acids are polar
Serine Threonine Cysteine Asparagine Glutamine (These are likely to have C-O or C-N bonds)
58
Which amino acids are positively charged
Lysine Hisidine Arginine (arginine and hisdine have a delocalised charge)
59
Which R groups are negatively charged
Aspartate Gluatamate
60
In solution, amino acids can ionise Which two groups allow this
Carboxyl and amine COOH will loose protons forming COO- NH2 will gain protons forming NH3+
61
Amino acids are amphoteric meaning
they can both donate and loose protons
62
How is the pKa of an amino acid measured if it is amphoteric
is the pH at which a group has equal amount of protonated and unprotoned forms So at pH below the pKa the group carries a positive charge
63
Why are we more concerned about the ionisation of the R groups of the amino acids rather than the carboxyl and amine groups
Because the carboxyl and amine groups are used to form peptide bonds
64
What is pKa in terms of amino acids
proton binding ability a low pKa meaning it has a low affinity for protons
65
Which amino acids are acidic at pH 7.4
Aspartic acid Glutamic acid
66
Give an example of two amino acids which are basic at 7.4 This means they will have a high affinity for protons
Arginine Lysine
67
What is a hydropathy value
It is the ability of an amino acid to dissolve within water High value = hydrophobic Low value = hyrdophillic
68
Which amino acids have a high hydropathy value = hydrophobic
Valine Leucine Isoleucine Methionine These amino acids are more likely to exist within the protein Bar tryosine, the aromatic R groups are also hydrophobic
69
Which amino acids are good for structure and why
Glycine and Alanine because they have really small R groups
70
Why is proline unique
It causes the back bone of the protein to kink
71
Why is cysteine unique
cysteine forms covalent disulphide bonds
72
What are the 4 fundamental forces of molecular biology
Electrostatic interactions (ionic) Polar interactions (hydrogen bond) Van der Waals interactions (dipole moment) Hydrophobic interactions (they are all non-covalent forces)
73
The 4 forces that operate in proteins are generate by the sequence of amino acids. They are crucial for ....
1. The chemical reactivity of protein as enzyme 2. The ability of a protein to fold into the correct shape (conforamtion) required to fulfill its function in the cell
74
How strong are non-covalent forces compared to covalent bonds
Are individually weak but collectively strong and flexible Numerous non-covalent and dynamic foces in and between macromolecules
75
What are electrostatic (ionic) interactions
These occur between atoms that are oppositely charged They are the strongest as ionic bonds form between fully charged ions However hydration by water can weaken their strength
76
Amino acids with charged amino acids can form electrostatic interaction Which onces are these
Aspartate Glutamate Lysine Arginine Histidine
77
What is the most important example of ionic bonds in proteins in human
ATPases Lysine amino acid R-group bonds ionically to adenosine triphosphate
78
What are polar bonds
Specialised type of polar interaction that involves a slightly electropositive hydrogen atom that interacts with a electronegative acceptor atoms Most hydrogen bonds in proteins occur between hydrogen and oxygen/nitrogen
79
What are polar bonds
Specialised type of polar interaction that involves a slightly electropositive hydrogen atom that interacts with a electronegative acceptor atoms Most hydrogen bonds in proteins occur between hydrogen and oxygen/nitrogen
80
Water forms two hydrogen bond per molecule Why is water very important to protein function:
Provide a solvation shell around the protein Control the ionic interactions between opposite charges by reducing them