The Foundations of Biochemistry (Lec 1) Flashcards

1
Q

Molecular Complementarity

A

Enables proteins with complimentary shapes and chemical properties to form biomolecular interactions

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2
Q

Chemical Building Blocks

A

Small molecule building blocks form larger cellular structures and polymers

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3
Q

Chemical Equilibrium

A

Chemical reactions are reversible. The ratio of forward (kf) and reverse (kr) reaction rate constants, reflects the relative amount of products and reactants at equilibrium

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4
Q

Chemical Bond Energy

A

Energy driving many cellular activities is derived from hydrolysis of the phosphoanhydride bond in ATP

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5
Q

Molecular Hierarchy of Structure

A

Monomeric Units (subunits) -> Macromolecules -> Supramolecular complexes -> The cell/organelles

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6
Q

Isomer

A

Molecules that share the same chemical formula but have a different arrangement of atoms

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7
Q

Stereoisomer

A

Isomers that have different physical properties

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8
Q

Geometric

A

Isomers that have different physical and chemical properties

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9
Q

Enantiomers

A

Isomers that have identical physical properties and react identically with achiral reagents (mirror images)

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10
Q

Diastereomers

A

Have different physical and chemical properties (non-mirror images)

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11
Q

Cis.

A

Isomers with Cis- indicates that the functional groups are on the same side of the carbon chain

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12
Q

Trans.

A

Isomers with Trans- indicates that functional groups are on opposing sides of the carbon chain

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13
Q

Biomolecule Interactions are…

A

SPECIFIC!

Macromolecules fold into 3D structures with unique binding pockets, allowing only certain molecules to fit in and bind

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14
Q

How to Speed Up Reactions

A
  1. Increase temp.
  2. Increase reactant concentration
  3. Change the reaction by coupling with a more efficient one
  4. Lower activation barrier through catalysis
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15
Q

Unfavourable Reactions

A

Requires energy (endergonic)

  • A reaction might be thermodynamically unfavorable (ΔG°> 0) and requires work and energy for order
  • A metabolic reaction might have too high an energy barrier (ΔG‡ > 0).
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16
Q

Favourable Reactions

A
Releases energy (exergonic)
- Breakdown of some molecules
17
Q

Energy Coupling

A

Chemical coupling of exergonic and endergonic reactions allows otherwise unfavourable reactions

18
Q

Catalysis

A

A catalyst is a compound that increases the rate of a chemical reaction by:
- lowering the activation energy ΔG‡

19
Q

Feedback Inhibition

A

In a process where multiple enzymes are at work, the product (or excess of a product) of the final enzyme inhibits an enzyme earlier in the cycle

20
Q

Central Dogma of Biochem

A

Gene on DNA strand -> transcribed into Messenger RNA -> translated into Polypeptide Chain -> folding of polypeptide chain into Native Structure

21
Q

Hydrogen Bonds

A

Strong dipole-dipole bond that arise between a covalently bound Hydrogen atom and a lone pair of electrons

  • Stronger bonds formed when atoms are in line
  • Weaker when atoms are bent at the bonds
22
Q

Water as a Solvent

A

Good solvent for charged and polar substances:
– amino acids and peptides
– small alcohols
– carbohydrates

Poor solvent for nonpolar substances:
– nonpolar gases
– aromatic moieties
– aliphatic chains (lipids)

23
Q

Amphipathic

A

Molecule consisting of both polar and non-polar functional groups

24
Q

Non-covalent Interactions: Ionic Interactions

A

Electrostatic interactions between permanently charged species, or between the ion and a permanent dipole

25
Q

Non-covalent Interactions: Dipole Interactions (H-Bonds)

A

Electrostatic interactions between uncharged but polar molecules that produce alpha helices and beta sheets

26
Q

Non-covalent Interactions: Van der Waals Interactions

A

Weak interactions between all atoms, regardless of polarity. Attractive (London dispersion) and repulsive (Steric repulsion) component

27
Q

Non-covalent Interactions: Hydrophobic Effect

A

Complex phenomenon associated with the ordering of water molecules (aqueous solution) around nonpolar substances

28
Q

Hydrophobic Effect favors Ligand Bonding

A

Binding sites in enzymes and receptors are usually hydrophobic, and such sites allow easy binding as water is displaced and entropy increases

29
Q

Origin of Hydrophobic Effect

A

Dispersion of lipids in H2O

  • non-polar tails of lipids exposed to ordered water molecules
  • entropy of system decreases

Clustering of lipids in H2O

  • non-polar portions aggregate so that fewer water molecules are ordered
  • increases entropy of system
30
Q

Ionization of Water (H2O -> H+ and OH-)

A

(H2O -> H+ and OH-)

O-H bonds are polar and can dissociate heterolytically, producing a proton (H+ ion) and a Hydroxide ion (OH-)

31
Q

Proton Hydration

A

Protons do not exist free in solution, they are rapidly hydrated to form hydronium ions (H3O+).

32
Q

Proton Hopping

A

Protons hop between series of hydrogen-bonded water molecules. As a Hydronium ion (H3O+) loses a proton (H+), a water molecule (H2O) gains one. Results in rapid net movement of protons over a long distance

33
Q

pH

A

pH is defined as the negative logarithm of the hydrogen ion concentration (pH = -log[H+]). In neutral solution, [H+] = [OH–] and the pH is 7.

34
Q

Dissociation of Weak Electrolytes

A

Weak electrolytes dissociate only partially in water, the extent of dissociation is determined by the acid dissociation constant Ka.

35
Q

pKa Measures Acidity

A

pKa is defined as the negative log of the dissociation constant. A lower pKa value indicates a stronger acid (acid more fully dissociated in water)

36
Q

pH = pKa

A

At pH = pKa, there is a 50:50 mixture of acid and anion forms of the compound. Buffering capacity of acid/anion system is greatest at pH = pKa