Section 1 Flashcards

bonding, thermodynamics and basics (50 cards)

1
Q

What is biochemistry?

A

The study of chemical substances and vital processes occurring in a living organism

Interested in how molecules interact with each other and themselves -> aka BONDING

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2
Q

What is a biomolecule?

A

An organic compound normally present as an essential component of living organisms

  • 4 types:
    - carbohydrates (sugars, storing energy, cellulose)
    - lipids (membranes, cholesterol [membrane fluidity], energy)
    - nucleic acids (DNA, genetic info, RNA, ATP)
    - proteins (enzymes, structure, transport, receptors, immune function)
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3
Q

What 5 elements make up most biomolecules?

A

CHNOPS (carbon, hydrogen, nitrogen, oxygen, phosphorus, sulphur)

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4
Q

Characteristics of a covalent bond

A

sharing of 2 e- between 2 adjacent atoms
About 1 Angstrom (1 x 10^(-10)m)

high bond energy
Short bond width
not easily reversible
Stable and strong interaction (only strong interaction)
NOT electrostatic
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5
Q

Carbon with 4 bonds is

A

tetrahedral
Bond angles 109.5 degrees
free to rotate bonds
Single bonds

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6
Q

aromaticity!

A

Pi conjugated bonding in a planar ring

resonance stabilized

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7
Q

Characteristics of a C=C bond

A

Atoms in single plane

Double bond conformationally restrained BUT atoms attached to C=C-X can rotate even though X

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8
Q

Describe an ionic interaction

A
  • 2nd strongest interaction
  • electrostatic
  • depends on molecule size, solvent and distance
    > interaction of 2 charged atoms based on Coulomb’s Law
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9
Q

Coulomb’s Law

A

F = q1-q2/Er^2

F -> force of interaction
E -> dielectric constant (takes into account medium atoms are in)
Ex.) water has high dielectric constant, surrounds molecules and decreases ionic interaction -> lowers ionic force between 2 charged atoms
q=charge on atom
R = radius between charges on atoms

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10
Q

Hydrogen bonding

A

Hydrogen atom partly unequally shared between 2 electronegative atoms (ELECTROSTATIC, partially ionic (10%))

  • H donor (which H is covalently bound to -> electronegative (partly - charged), pulls e- away from H, making it partly + charged)
  • H acceptor is also electronegative and develops partial - charge or could be ionically charged
    • needs to have lone pair or charge -> can’t be resonance stabilized

> H+ (partly + charged) attracted to electronegative acceptor and H bond is formed

H BOND DONOR AND ACCEPTOR ARE USUALLY O, N AND S

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11
Q

How strong and long are hydrogen bonds?

A

Strength: 4-13 KJ/mol
Length: 1.5-2.6 Angstroms

0.117nm vs covalent = 0.0965 nm

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12
Q

What is one example of a negative type non-covalent interaction?

A

Electrostatic repulsion of phosphate groups in DNA backbone

  • contributes to shape of DNA
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13
Q

Examples of H bonds

A

carbonyl -> O-H
Amino -> O-H
ester -> O-H

Amino-H -> carbonyl
amino-H -> ester
Amino-H -> -N=

complimentary base pairs in DNA

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14
Q

Van Der Waal Interactions

A
  • electrostatic interaction of temporary dipoles in any 2 molecules
  • attraction lasts until atomic clouds repel eachother
  • cause distortion of electron cloud
  • occur at Van Der Wall contact distance -> distance of maximal attraction between 2 atoms
    > atoms will start to repel each other if clouds overlap or won’t be close enough to interact if too far
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15
Q

How strong is a van Der waal interaction and where can it occur?

A
  • 2-4 kJ/mol
  • distance between DNA base pairs is van Der waal contact distance
    • maximized intermolecular attraction
    • contributes to the stability
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16
Q

Describe the Van Der Waal Graph

A

as we bring atoms closer they experience attraction past a key distance, then the most attraction at Van Der Waal Radius.

  • then repulsion because election clouds repel each other
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17
Q

What medium do most biomolecular reactions occur in?

A

Water

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18
Q

What happens as a result of all the H-bonding capability of water?

A

Very cohesive - forms many H bonds with itself

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19
Q

What gives water its H-bonding capability?

A

Can act as H bond acceptor (x2) and H bond donor (x2) -> bent shape and 2 electron lone pairs

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20
Q

Why is water an excellent solvent for polar molecules (hydrophilic)?

A

Can weaken the electrostatic interactions between polar molecules by H-bonding with them -> competing for their charge against themselves

> reduces the electrostatic interactions up to 80x with high dielectric constant

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21
Q

hydrophobic molecules

A

Water-fearing -> not soluble in water

22
Q

amphipathic

A

contains both hydrophobic and hydrophilic bits

23
Q

Why is water a double-edged sword?

A
  • can dissolve things

- interferes with electrostatic interactions of molecules (eg. H-bonding or ionic interactions)

24
Q

first law of thermodynamics

A

the total energy of a system and its surroundings stays constant

energy can’t be created or destroyed but its form can change

25
enthalpy (H)
heat content of the system
26
2nd law of thermodynamics
total energy of a system and its surroundings is always increasing for a spontaneous process
27
entropy (S)
measure of randomness
28
When can the entropy of a local system be acceptably decreased?
When the entropy of the surroundings/universe increases by the same or greater amount eg.) when strands of DNA anneal, heat is released and the entropy of universe increases to counter decreased entropy of annealed strands
29
spontaneity
how likely a reaction is to occur (doesn't tell anything about speed)
30
spontaneity equation
deltaGsys = deltaHsys - T(K) x deltaSsys
31
What is G and why is it important?
Gibbs free energy -> KJ/mol > reactions need to be spontaneous to occur in a cell
32
endergonic reaction
delta G is positive - non-spontaneous
33
exergonic reaction
delta G is negative - spontaneous
34
equilibrium
when delta G is zero
35
What happens where the reaction is exothermic (delta H < 0)
delta G leans towards negative | -reaction becomes more likely to occur
36
What happens when delta S is positive?
reaction is more disordered and leans towards spontaneity
37
hydrophobic effect
- driven by increasing entropy of water - water molecules forced in a smaller SA cage (greater entropy) caused by gathering of nonpolar compounds together (aggregate) - less water in cage -> more random and offsets addition of lipids
38
Buffer
mixture of a weak acid and its conjugate base (with charged/uncharged groups depending on pH) - requires a weak acid that does not completely ionize in water - resists changes in pH in buffering region
39
Kw
ionization constant of waater -> 1 x 10^(-14) = [H+][OH-]
40
What are some qualities of pH scale?
pH = -log[H+] | - goes from 0 (strongly acidic) to 14 (strongly basic)
41
Ka
tells us when [acid]=[conj base] - when acid begins to dissociate (lose its proton) - Ka = [A-][H+]/[HA]
42
pKa
- low pKa is stronger acid | - pKa = -logKa
43
what is the pKa of acetic acid (acetate is conj base)?
4.8
44
Henderson-Hasselbach Equation
pH = pKa + log{A-}/{HA}
45
when pH < pKa when ph = pKa when pH > pKa
- > [HA} > {A-} - > [HA] = [A-] - > [HA] < {A-]
46
normal buffering range of buffer
+/- 1 pH unit on either side
47
When can buffers fail?
When you're outside the buffering region or when there is only acid or conj base
48
3 key buffers in conj base systems
1. carbonate/bicarbonate buffer CO2 + H2O = H2CO3 (carbonic acid) = H+ + HCO3- (bicarbonate) -> pKa => 6.1 2. phosphate buffer H2PO4- (dihydrogen phosphate ion) = H+ + HPO4-2 (monohydrogen phosphate ion) -> pKa => 6.9 3.) free amino acids can use histidine and cysteine
49
what guard systems does the body have for acidosis?
pKa of buffer system is slightly below pH of body to avoid acidosis since there is more conjugate base to soak up acid
50
how does a buffer work?
- if pH is too low, the addition of OH- will affect water instead of the weak acid to steal a proton and be neutralized (H+ + OH- = H2O), and pH rises sharply - when pH is within buffering range, adding H + or OH- will take proton or give proton to acetic acid/acetate, which are in equilibrium with each other - once acetic acid is all used up, it can't give protons to OH- and neutralize it to H2O so pH rises sharply