CBI Notes Flashcards

1
Q

What does the letter Z represent?

A

Atomic number

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2
Q

What is the unit for atomic mass?

A

Dalton (Da)

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3
Q

Define ionisation energy

A

Energy to remove an electron

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4
Q

Define electron affinity

A

Energy change when you add an electron to an element in it’s ground state

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5
Q

Electronegativity

A

Power of an atom to attract electron (~ IE and EA average)

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6
Q

How many known elements are there?

A

118

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7
Q

What do quantum numbers describe?

A

Atomic orbitals

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8
Q

What are the 4 quantum numbers?

A

Principal (n)
Orbital (azimuthal) (l)
Magnetic (ml)
Spin (ms)

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9
Q

What does the principle (n) define?

A

Shell

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10
Q

What does the azimuthal (l) define?

A

Orbital shape (s, p, d or f)

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11
Q

What does the magnetic (ml) define?

A

Number and orientation of the orbital shapes in a subshell

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12
Q

What does the spin (ms) define?

A

Spin direction

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13
Q

How can quantum numbers be calculated?

A

Calculating the solutions to wave functions

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14
Q

What are the possible values of the azimuthal number?

A

l = 0, 1, 2… (n-1)
where n is the principal number

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15
Q

In which sub shell is an electron with l=0

A

s

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16
Q

In which sub shell is an electron with l=1

A

p

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17
Q

In which sub shell is an electron with l=2

A

d

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18
Q

In which sub shell is an electron with l=3

A

f

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19
Q

What are the potential values of the magnetic quantum number (ml)?

A

0, +/- 1, +/- 2, … +/- l

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20
Q

What is a degenerate subshell?

A

Subshells with equivalent energy despite varying orientation (i.e. px, py and pz are degenerate)

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21
Q

Define the Pauli Exclusion Principle

A

No 2 electrons can have the same set of four quantum numbers

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22
Q

Define the Aufbau Principle?

A

The lowest orbital (least energy) is first occupied

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23
Q

Define Hund’s Rule

A

Electrons will fill separate orbitals in the same subshell before pairing up, unpaired electrons will have the same spin

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24
Q

Define Madelung’s rule

A

Some energy levels have overlaps (i.e.: 4s < 3d)

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25
Q

Define electronegativity

A

The power of an atom to attract electrons to itself

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26
Q

Define a cation

A

+/ve ion

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27
Q

Define an anion

A

-/ve ion

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28
Q

How is an “ionic bond” (lattice) defines?

A

A bond where EN>2

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29
Q

What is the net effect of ionic bonding?

A

Ionic lattice

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30
Q

Define covalent bonding

A

Electrons in the outermost shell are shared

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31
Q

What is a bonded pair (covalent bonding)?

A

Shared e-

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32
Q

What is a lone pair (covalent bonding)

A

Unshared e-

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33
Q

What does a significant difference in electronegativity (but <2) suggest?

A

Polar covalent bonding

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34
Q

Define molecule (IUPAC definition)

A

A molecule is an electrically neutral entity consisting of more than one atom

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35
Q

Difference between molecular and empirical formula

A

Molecular indicates how many of each atom is present but empirical shows proportion

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36
Q

What is the convention in the order that elements in organic molecules are written?

A

C(x)H(y) and then alphabetical order

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37
Q

What is the convention in the order that elements in ions are written?

A

+/ve ion first, -/ve ion second

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38
Q

What are the conventions in the writing of oxides?

A

End with O

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39
Q

What are the conventions in the writing of acids?

A

Start with H

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40
Q

What are the conventions in the writing of hydroxides?

A

End with OH

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41
Q

What does the condensed structural formula suggest?

A

The order molecules are in

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42
Q

What does the skeletal formula represent?

A

The shape of bonds and only some explicit atoms (most Cs and Hs are implicit)

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43
Q

What is VESPR theory?

A

It is used to predict the 3D shape of a molecule

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44
Q

What is the tetrahedral bond angle?

A

109.5

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45
Q

What is the bonding angle with 4 electron domains but 1 is a lone pair (i.e.: ammonia)?

A

106.6

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46
Q

What is the bonding angle with 4 electron domains but 2 are lone pairs (i.e.: water)?

A

104.5

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47
Q

Which are more repulsive, bonding or lone pairs?

A

Lone pairs

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48
Q

Which type of bonds are present in a double bond?

A

1 sigma and 1 pi

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49
Q

Which type of bonds are present in a triple bond?

A

1 sigma and 2 pi

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50
Q

Which type of bonds are present in a single bond?

A

1 sigma

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51
Q

What is VB theory?

A

Valance bond theory is that bonding requires subatomic orbital hybridisation

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52
Q

What is MO theory?

A

Molecular orbital theory predicts bond lengths and energies bit is complex with larger molecules

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53
Q

How much is 1 mol?

A

6.02e23

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54
Q

What does high Ka (dissociation constant) suggest for an acid?

A

Strong

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55
Q

What does low Ka (dissociation constant) suggest for an acid?

A

Weak

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56
Q

What dissociation do strong acids have?

A

Full

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57
Q

What dissociation do weak acids have?

A

Weak

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58
Q

What combines well to produce a buffer?

A

A weak acid and it’s conjugate base or a weak base and it’s conjugate acid

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59
Q

Withing which range do buffers work?

A

pH ranges approximately similar (+/- 1) to their pKa

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60
Q

How is a buffer produced?

A

Weak acid + salt of that acid
Weak base + salt of that base

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61
Q

How many stereoisomers does a molecule have?

A

2^n
where n is the number of stereoisomers

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62
Q

What are the Cahn-Ingol-Prelog rules for naming enantiomers?

A
  • Assign priority (Z) based on atomic weight
  • If there is a tie go out to the next furthest atom
  • The lowest priority faces into the paper
  • If the others are arranged clockwise -> R
  • If the others are arranged anticlockwise -> S
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63
Q

What is the CORN rule for naming amino acid enantiomers?

A
  • Orientate the molecule such that the H on the central C faces into the page
  • Other groups face outward
  • If they spell CORN clockwise they are D amino acids, if they spell it anticlockwise they are L
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64
Q

Describe the optical activity of enantiomers

A

Equal and opposite

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65
Q

Describe Z isomerism

A

Higher priority molecules on the same side of a double bond

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66
Q

Describe E isomerism

A

Higher priority molecules on either side of the double bond

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67
Q

What are examples of non-covalent interactions?

A

Permanent dipoles
London dispersion forces
Hydrogen bonds
Ionic interactions
Hydrophobic interactions
Steric interactions

68
Q

Which non-covalent forces are considered Van de Waals?

A

Permanent dipoles
London dispersion forces
Hydrogen bonds
Ionic interactions

69
Q

What increases the size of a London dispersion force?

A

Larger molecule

70
Q

Which molecules form hydrogen bonds?

71
Q

Law of conservation of energy

A

Energy cannot be created or destroyed, only transferred from one form to another

72
Q

What is true if delta G <0?

A

Spontaneous and exergonic

73
Q

What is true if delta G >0?

A

Non spontaneous endergonic

74
Q

What is true if delta G =0?

A

Chemical equilibrium

75
Q

What change in enthalpy (H) do favourable reactions have?

76
Q

What change in entropy (S) do favourable reactions have?

77
Q

What does an equilibrium constant (K)>1 suggest?

A

Forward reaction favoured

78
Q

What does an equilibrium constant (K)<1 suggest?

A

Backwards reaction favoured

79
Q

What is the second law of thermodynamics?

A

The entropy of the entire universe will increase oover time

80
Q

What does delta H>0 suggest?

A

Endothermic

81
Q

What does delta H<0 suggest?

A

Exothermic

82
Q

Which are the most common biological redox pairs?

A

NADH/NAD+ and FAD/FADH2

83
Q

How is NAD+ reduced?

A

Nicotinamide ring acts as an e- acceptor

84
Q

How is FAD reduced?

A

FAD ring acts as an e- acceptor

85
Q

What do chemical catalysts do?

A

They lower the energy required to overcome the transition state by providing an alternative reaction pathway

86
Q

What does delta S>0 suggest?

A

Increase in ways for energy to be dispersed

87
Q

What does delta S<0 suggest?

A

Decrease in the ways for energy to be dispersed

88
Q

What’s Hess’ Law?

A

Total enthalpy change for a given reaction is independent of reaction pathway

89
Q

Which step of an SN1 reaction is rate determining?

A

The first step has the highest Ea

90
Q

Which step of an SN2 reaction is rate determining?

A

It’s a one step reaction

91
Q

Which type of substitution reaction has a carbocation intermediary?

92
Q

Which type of substitution reaction may lead to stereoinversion?

93
Q

Which type of substitution reaction is biologically more common?

94
Q

What are the 4 major categories of biomolecules?

A

Sugars
Lipids
Nucleotides
Amino acids

95
Q

What is the polymer of sugars?

A

Polysaccharide

96
Q

What is the polymer of nuceleotides?

A

Nucleic acids

97
Q

What is the polymer of amino acids?

98
Q

What is the general structure of carbohydrates?

99
Q

What are the two types of monosaccharide?

A

Aldose
Ketose

100
Q

In which form are carbohydrates found in water?

A

They can interconvert between ring and linear

101
Q

How do monosaccharides bond?

A

Condensation reactions to form glycosidic linkages

102
Q

Which are the lipid classes?

A

Fatty acid
Triacylglycerols
Sterol lipids
Glycerophospholipids
Sphinolipids

103
Q

How would we write the name of a fatty acid with 18 carbons and 3 double bonds?

104
Q

How do we describe the location of a double bond in a fatty acid which is 6 carbons from the end CH3?

A

w-6 or n-6

105
Q

How do we describe the location of a double bond in a fatty acid which is 6 carbons from the COOH?

A

18:1(6) or C-6
(in an 18 C and 1 double bond chain)

106
Q

Which lipid is common in adipocytes?

A

Triacylglyerols

107
Q

Which lipid is common in membranes?

A

Glycerophospholipids

108
Q

What is true about flip-flop in accordance with the Singer model?

A

It’s unfavourable and rare

109
Q

Which phase do saturated lipids favour in the membrane?

110
Q

Which phase do unsaturated lipids favour in the membrane?

111
Q

How does cholesterol regulate membrane fluidity?

A

Stabilises at high temp
Prevents stiffening at low temp

112
Q

What is Tm?

A

The temperature at which membranes transition between solid and liquid phases

113
Q

What type of bond forms between guanine and cytosine?

A

Triple hydrogen bond

114
Q

What type of bond forms between adenine and thymine/ uracil?

A

Double hydrogen bond

115
Q

Give examples of monomeric nucleotides?

A

ATP and GTP

116
Q

How do nucleotides bond to form DNA?

A

Condensation reaction
Bonds form between the 3C and phosphate group

117
Q

What groups are present in an amino acid?

A

R group
COOH carboxyl
NH2 amine group

118
Q

What are the 4 classifications of amino acid?

A

Neutral, non-polar
Neutral, polar
Basic
Acidic

119
Q

What does the primary protein structure define?

A

Structure and function

120
Q

What bonds form in primary protein structure?

A

Peptide (-CO-NH-) bonds

121
Q

What bonds form in secondary protein structures?

A

H interactions (between carbonyl and nitrogen atoms)

122
Q

What are the potential secondary structures of polypeptides?

A

Beta sheets
Alpha helices
Hairpin bends
Beta turns

123
Q

What determines tertiary folding of a protein?

A

R group interactions

124
Q

What determines quaternary interactions?

A

Additional polymers/ molecules

125
Q

Name 4 protein purification techniques

A

SEC (size-exclusion chromatography)
IEC (ion-exchange chromatography)
Affinity chromatography
SDS-PAGE

126
Q

Describe SEC

A

SEC (size-exclusion chromatography) consists of passing a liquid through a column of porous beads, the smaller molecules will take longer as they will enter the pores but the larger molecules will pass through faster.

127
Q

Describe IEC

A

IEC (ion-exchange chromatography) passes liquid through a column which has beads treated to certain charges to interact with proteins passing through

128
Q

Describe affinity chromatography

A

Tags in a column interact with the matrix which traps the proteins in the column. This can later be washed out

129
Q

Describe SDS-PAGE

A

Molecules are treated by with SDS detergent to make them -/ve. They are then placed between the anode (+) and cathode (-) and they travel towards the anode with the smallest arriving last

130
Q

Hiii

131
Q

What is the function of biological catalysts?

A

Lower the energetic barrier to allow a reaction to proceed

132
Q

Where can Delta G be shown on a reaction pathway?

A

Instead if Ea

133
Q

How do we classify enzyme names?

A

By 4 numbers

134
Q

What is Vmax?

A

The point at which all enzymes are occupied by substrates

135
Q

What is Km ?

A

A constant which defines the catalytic properties of an enzyme

136
Q

What is the Michaellis-Menten equation?

A

An equation which describes the variation of enzyme activity as a function of substrate concentration

137
Q

What does a high KM suggest about substrate affinity?

A

Low as a lot of substrate is required to reach Vmax

138
Q

What does a low KM suggest about substrate affinity?

A

High as a small concentration of substrate is required to reach Vmax

139
Q

What do Lineweaver-Burk plots show?

A

A double reciprocal of a Michaelis Menten plot which allows us to calculate Vmax ad KM

140
Q

How is a Lineweaver-Burk plot used to calculate Vmax?

A

The y-intercept is 1/Vmax

141
Q

How is a Lineweaver Burk plot used to calculate KM?

A

The root = -1/KM

142
Q

What is k(cat)?

A

The max turnover of a saturated enzyme/second

143
Q

What does a high k(cat) suggest?

A

Greater efficiency

144
Q

What dies a low k(cat) suggest?

A

Lower efficieny

145
Q

Describe a competitive inhibitor

A

Resembles the substrate but can be overcome by a higher substrate concentration

146
Q

Describe an uncompetitive inhibitor

A

Binds to the formed complex and prevents product release and cannot be overcome

147
Q

Describe a non-competitive inhibitor

A

Binds to the allosteric site and prevents catalyst if function

148
Q

How do KM and Vmax change in the presence of a competitive inhibitor?

A

Apparent increase in KM
No change in Vmax
(A higher substrate concentration is required for the same reaction)

149
Q

How do KM and V max change in the presence of an uncompetitive inhibitor?

A

Apparent decrease in KM and Vmax by the sane extent
(As ESI complex is forming but not being release)

150
Q

What is the effect of a non-competitive inhibitor on KM and Vmax?

A

KM stays the same
Vmax decreases
(less e=substrate is available to complete it’s function)

151
Q

When may cofactors be important in catalytic activity?

A

These are vitamin-derived organic molecules such as NAD+ or FAD which may be necessary to initiate catalytic activity.

152
Q

Why do high temperatures denature enzymes?

A

Break tertiary and secondary structure bonds

153
Q

What type of inhibition is allosteric?

A

Primarily non-competitive but other kinds can be too

154
Q

What shape is the Michaelis Menten enzymatic profile for allosteric-regulated enzymes?

A

Sigmoidal due to high sensitivity

155
Q

Where does the Kreb’s cycle occur?

A

Mitochondrial matrix

156
Q

Which part of respiration is anaerobic?

A

Glycolysis

157
Q

Where does glycolysis occur?

158
Q

What are the steps in respiration?

A

Glycolysis
Oxidative decarboxylation
TCA
ETC
OXPHOS

159
Q

What are the steps in oxidative decarboxylation?

A

Decarboxylation
Oxidation
Transfer to CoA

160
Q

What enzyme catalyses oxidative carboylation?

A

Pyruvate dehydrogenase

161
Q

Where does glycolysis occur?

162
Q

Where does glucogenesis occur?

A

Primarily in the Cytosol

163
Q

Define glycolysis

A

The breakdown of glucose resulting in the production of two pyruvate molecules

164
Q

What are the steps in glycolysis?

A

Trapping glucose
Cleavage into 3C unit
Pay-off

165
Q

Which steps in glycolysis are not reversible?

A

Step 1: 1 and 3
Step 3: last step