1.1 Amino acids and peptides Flashcards

1
Q

What is the simple definition of Gibbs free energy?

A

It is the energy of the reaction available to do work

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2
Q

What is the equation relating the change in gibbs free energy to heat and entropy?

A
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3
Q

How are spontaneous reactions defined in terms of delta G?

A

Spontaneous reactions have a negative delta G

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4
Q

What is the difference between exergonic and endergonic?

A
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5
Q

What is the difference between exothermic and endothermic?

A
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6
Q

whats up

What does the sign of delta S indicate in terms of the change in entropy?

A

􏰀Delta S is negative: less disorder

Delta 􏰀S is positive: more disorder

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7
Q

What is the equation linking delta G and delta G*?

A
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8
Q

How does the position of equilibrium relate to the change in Gibbs free energy?

A

The further away from equilibrium you start, the more work is done before you get there.

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9
Q

What are some ways through which a negative delta G can be achieved?

A
  1. Negative delta H (exothermic)
  2. Positive delta S (increase in entropy)
  3. Any combination that leaves delta G negative
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10
Q

What are the standard conditions in chemistry?

A
  1. 298 K
  2. Gases at a partial pressure of 101.3 kPa (1 atm)
  3. Reactants and products at 1 M concentrations
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11
Q

What are the standard conditions in biochemistry?

A

Same as those of chemistry but the reaction occurs in a well buffered aqueous solution at pH 7 with [H+] ion concentration 10-7 and Mg2+ = 1mM

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12
Q

If you look at the free energy equation and set all initial concentrations to 1, what happens?

A

Shows delta G is equal to delta Go when everything is at standard conditions

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13
Q

How does the free energy equation change when all concentrations are at equilibrium?

A

At equilibrium delta G=0 this means the reaction can do no more work.

This shows that delta G0 is a constant

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14
Q

What is used to predict where a reaction will be spontaneous?

A

The measure of whether a reaction will proceed spontaneously is delta G not delta Go.

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15
Q

How can the initial conditions of a reaction be altered in order to get a spontaneous reaction?

A
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16
Q

What are three ways of making unfavourable reactions go?

A
  • Remove one or more of the products at a rate much faster than it is produced so that the reaction is now kinetically driven
  • Replenish one or more of the reactants at a much faster rate than it is removed
  • Couple the unfavourable reaction with a highly favourable reaction (in the active site of an enzyme)
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17
Q

Label the blanks on this ATP molecules

A
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18
Q

What is the difference between a nucleotide and nucleoside?

A

Nucleotide = base + sugar + phosphate

Nucleoside = base + sugar

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19
Q

What causes the release of energy via ATP?

A

Energy is released upon the hydrolysis of phosphoanhydride bonds

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20
Q

Show the equation for the release of energy via ATP including delta G

A
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21
Q

How is bond energy related to bond breakage/forming?

A

Energy is required to break any bond

Energy is released when any bond forms

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22
Q

Why is energy required to break any bond?

A

The bonded state is a more stable state that’s why it required energy to break

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23
Q

Why is the ATP reaction highly exergonic?

A
  • ATP has a higher negative charge density than ADP (ATP less stable)
  • Pi is very stable: multiple resonance states exist
  • ATP phosphoanhydride bonds are relatively weak
  • ADP phosphoanhydride bonds and Pi bonds are relatively strong
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24
Q

Why is tri phosphtate less stable than di phosphate?

A

Due to charge density, are there is a great accumualtion of negative charges and more strain and repulsion

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25
What are some of the roles of proteins in the body?
* Catalysis * Transport * Structure * Motion * Signaling
26
What are some of the properties that make amino acids well suited to carry out a variety of biological functions?
* Capacity to polymerise * Useful acid base properties * Varied physical properties * Varied chemical functionality
27
What is the basic structure of an amino acid?
The 􏰿 carbon always has four substituents and is tetrahedral. All (except proline) have: – an acidic carboxyl group connected to the 􏰿carbon – a basic amino group connected to the 􏰿carbon – a alpha hydrogen connected to the􏰿 carbon
28
Which protein isomer is found in naturally occuring amino acids?
L amino acids
29
Where do the D and L names for amino acids originate from?
Based on the rotation of plane of polarised light viewed towards the light source or based on what you could chemically synthesise them from
30
How can you determine the chirality of the alpha carbon?
31
What amino acid is this?
Alanine
32
Alanine
What amino acid is this?
33
Cysteine
34
Aspartate
35
Glutamate
36
Phenylalanine
37
Glycine
38
Histidine
39
isoleucine
40
Lysine
41
Leucine
42
Methionine
43
Asparagine
44
Proline
45
Glutamine
46
Arginine
47
Serine
48
Threonine
49
Valine
50
Tryptophan
51
Tyrosine
52
53
# Reversed prompt draw the amino acid Cysteine
54
# Reversed prompt draw the amino acid Aspartate
55
# Reversed prompt draw the amino acid Glutamate
56
# Reversed prompt draw the amino acid Phenylalanine
57
# Reversed prompt draw the amino acid Glycine
58
# Reversed prompt draw the amino acid Histidine
59
# Reversed prompt draw the amino acid isoleucine
60
# Reversed prompt draw the amino acid Lysine
61
# Reversed prompt draw the amino acid Leucine
62
# Reversed prompt draw the amino acid Methionine
63
# Reversed prompt draw the amino acid Asparagine
64
# Reversed prompt draw the amino acid Proline
65
# Reversed prompt draw the amino acid Glutamine
66
# Reversed prompt draw the amino acid Arginine
67
# Reversed prompt draw the amino acid Serine
68
# Reversed prompt draw the amino acid Threonine
69
# Reversed prompt draw the amino acid Valine
70
# Reversed prompt draw the amino acid Tryptophan
71
# Reversed prompt draw the amino acid Tyrosine
72
What is the three letter code for aspartate?
D and Asp
73
What is the three letter code for glutamate?
E and Glu
74
What is the letter codes for phenylalanine?
F and Phe
75
What is the three letter code for isoleucine?
I and ile
76
What is the three letter code for Lysine?
K or Lys
77
What is the three letter code for asparagine?
N or Asn
78
What is the three letter code for glutamine?
Q or Gln
79
What is the three letter code for Arginine?
R or arg
80
What is the three letter code for tryptophan?
W or trp
81
What is the three letter code for tyrosine?
Y or Tyr
82
Which amino acids belong to the non polar aliphatic R groups?
Glycine, alanine, proline, valine, Leucine, Isoleucine, methionine
83
Which amino acids belong to the polar, uncharged R group category?
Serine, Threonine, Cysteine, Asparagine, Glutamine
84
Which amino acids belong to the aromatic R groups?
Phenylalaline Tyrosine Tryptophan
85
Which amino acids belong to the positively charged R groups? (basic)
Lysine Arginine Histidine
86
Which amino acids belong to the negatively charged R groups?
Aspartate Glutamate
87
When is pKa equal to pH?
88
For the acidic side chains of aspartic acids and glutamic acid, in what state do these R groups exist at physiological pH?
Their pKa is 4.4 so at neutral pH they are completely ionsided and negatively charged
89
In what state do the basic side chains of Lysine and Arg have their R groups at physiological pH?
Lys has a pKa of 10 so the protonated, positively charged form dominates Arg has a pKa of 12 so similarly completely ionised.
90
What are the special properties of basic side chain Histidine?
* HIghly used in enzyme active sites * The imidazole ring is a H bond done or acceptor (electrophile or nucleophile) and chemically ambidextrous * Effective nucleophile in its deprotonated form
91
What are some properties of the amide side chains asparagine and glutamine?
* Not very chemically reactive * Polar * H bond donor and acceptor * THe can remove amide group to become carboxylic acids
92
What state does Tyrosine's aromatic side chain exist at physiological pH?
* The phenol form dominates above pH 10, but below it phenolate is negatively charged
93
Why are the aromatic side chains responsible for UV absorbance and fluorescence properties?
* The extent and geomtery of conjugated double bond systems cause spectral differences
94
What properties does proline hold due to its unique geometry?
* It has no NH group so its an imino acid * Can't act as a backbone H bond donor * Limites rotation between N-Cæ angle -60o
95
Compare the two sulfur containing side chains, cysteine and methionine
96
What are some examples of disulfide bonds being seen in proteins?
97
98
What are the rotation properties of the peptide bonds?
* The peptide bond has partial double bond character due to resonance * Rotation around CO-NH bond is not free, groups are co-planer
99
What can be said about the size of the peptide bond?
100
Which peptide bond isomer is favoured energetically?
* The trans form is intrinically favoured energetically * Due to severse steric hindrance (van der Waals) repulsion of the side chain in cis
101
What sort of peptied bond isomerisation is found in proline?
Similar steric hindrance in trans and cis but trans is still favoured for steric reasons
102
Label the terminology of the peptide bond
103
What happens when the peptide linkage is cis in nature? For bond angle
104
Label which one is the phi and si angle
105
Fill in the blanks about the phi angle
106
Fill in the blanks about the psi angle
107
Why are phi and psi so important?
Because assuming all peptide bonds are trans then all the conformation freedom in the backbone of the polypeptide is due to these two rotations, everything else is fixed
108
Fill in the blanks about side chain dihedral angles