UNIT 4 CONCISE FL EASY Flashcards

(46 cards)

1
Q

Enzyme def?

A
  • Protein biocatalyst, lowers activation energy.
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2
Q

Active site?

A
  • Specific 3D region binds substrate.
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3
Q

Enzyme Specifity?

A
  • Due to active sites unique shape complementary to the substrate.
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4
Q

Optimum temperature?

A
  • Temperature for maximal enzyme activity.
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5
Q

Denaturation ( high temperature) def?

A

-Breaks weak non-covalent bonds (H-bonds, ionic, dispersion) in 3D structure.

  • Active site loses shape=Enzyme activity lost.
  • Generally irreversible.
  • Primary structure (peptide bonds) remains intact.
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6
Q

Denaturation (extreme pH) def?

A
  • Alters R-group ionisation, disrupting ionic/H-bonds in 3D structure.
  • Active site loses shape=Enzyme activity lost.
  • Generally irreversible.
  • Primary structure (peptide bonds) remains intact.
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7
Q

Deactivation (low temp) def?

A
  • Deactivation (Low Temp): Lower kinetic energy, decreased frequency successful collisions per unit time; enzyme activity reduced; reversible; not denaturation.
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8
Q

Optimum pH def?

A
  • pH for maximal enzyme activity; specific for each enzyme.
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9
Q

Stereoisomers def?

A
  • Same structural AND SEMI STRUCTURAL formula, BUT A DIFFERENT SPATIAL OR 3D atomic arrangement.
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10
Q

Optical Isomers def?

A
  • Stereoisomers that are non-superimposable mirror images AND rotate plane-polarised light in opposite directions.
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11
Q

Enantiomers def?

A
  • A pair of optical isomers that are non-superimposable mirror images. AND rotate plan-polarised light in opposite directions.
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12
Q

Chiral compound def?

A
  • Molecule non-superimposable on its mirror image.
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13
Q

Chiral carbon def?

A
  • Carbon atom bonded to four different groups. (Causes chirality).
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14
Q

Method of separation to separate enantiomers?

A
  • Chiral High-Performance Liquid Chromatography (HPLC).
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15
Q

Enantiomer separation (drug synthesis) crucial for?

A
  • Drug safety (preventing inactive/toxic enantiomer).
  • Drug efficacy (ensuring correct, active enantiomer).
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16
Q

Competitive inhibitor(CEI) def?

A
  • Molecule that binds to and occupies the enzyme’s active site.
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17
Q

Mechanism of a CEI def?

A
  • Prevents substrate binding, thus blocking reaction.
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18
Q

Structure of a CEI def?

A
  • Must be structurally similar to substrate to fit active site.
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19
Q

Steams distillation used for?

A
  • Essential oils avoid thermal decomposition.
20
Q

Simple distillation used for?

A
  • > 25 deg celcius difference in boiling points.
21
Q

Fractional distillation used for?

A
  • < 25 deg celcius.
22
Q

Solvent extraction def?

A
  • Method of separating compounds based on a difference in solubility in two compounds.
23
Q

Immiscible def?

A
  • A set of liquids that do not mix with each other.
24
Q

Achiral compound def?

A
  • Compound with a superimposable mirror image.
25
Features of medicinal molecules def?
- Relatively large molecules. - Contain a polar group. - Contain rings.
26
Common polar solvents def?
- Water. - Ethanol.
27
Common non-polar solvents def?
- Hexane. - Ether.
28
Solvents with limited polarity include def?
- Acetone. - Dichloromethane.
29
In simple distillation why are anti-burning granaries ( boiling chips) added def?
- To distribute heat and avoid explosion.
30
Explain when a heating mantle would be prefered over a bunsen burner def?
- If a substance is flammable e.g. ethanol , then a heating mantle is used instead of a bunsen burner to avoid explosion.
31
IGNORE THIS FLActive ingredient def?
NOPE DONT NEED TO DO THIS
32
Primary structure, bonding and strength during denaturation def?
- Structure: Linear sequence of amino acids. - Bonding: Covalent peptide bonds (between - NH2 of one and - COOH of another). - Stability: Strongest level; intact during denaturation.
33
Secondary structure bonding and strength during denaturation def?
- Structure: Local, regular folding of polypeptide backbone ( alpha -helix, beta-pleated sheet). - Bonding: Weak non-covalent hydrogen bonds between backbone N-H and C=O and groups. - Stability: Broken by denaturation.
34
Tertiary structure bonding and strength during denaturation def?
- Structure: Overall 3D folding of a single polypeptide chain. - Bonding: Interactions between R-groups (side chains): - Weak non-covalent: Hydrogen bonds, ionic interactions (salt bridges), dispersion forces. - Strong covalent: Disulfide bridges (-S-S) between two cysteine residues.
35
Quaternary structure def?
- The combination and interactions between two or more tertiary chains. HOWEVERY NOT ALL PROTEINS HAVE QUATERNARY STRUCTURES.
36
Which type of boning is found in both secondary and tertiary structures of a protein def?
- Hydrogen bonding.
37
What is the strongest intermolecular bonding that could involve the residue of any amino acid def?
- Ionic interactions.
38
2 methods to increase the rate of solvent extraction def?
- Increase the temperature of the solvent extraction if the compounds are thermally stable. - Grinding or lending the leaves to break up the plant and increase the surface area.
39
Explain why once ethanoic acid is extracted using solvent extraction, the extract is not typically purely 100% ethanoic acid?
- Because all of the compounds of the same polarity will be extracted no just the compound of interest.
40
Another organic chemist suggested the use of HPLC to separate the extract and obtain pure ethanoic acid.Determine if HPLC would be successful in isolating ethanoic acid. Justify your answer?
- Yes. - Justification: HPLC separates compounds based on their differential affinities for the stationary and mobile phases, leading to distinct retention times that allow for their isolation.
41
Formula to find the number of enantiomers and stereoisomers are?
- 2 to the power of chiral carbons.
42
Discuss how it is possible that only one of the stereoisomers is biologically active as a heart medication?
- Stereoisomers= different spatial/3D atomic arrangement. - As a result only one of them will have a shape that would be SPECIFIC and Complementary to the target molecule/enzyme.
43
CYS-CYS bond indicates what type of protein structure and bonding?
- A Cys-Cys bond (specifically, a disulfide bridge or disulfide bond) indicates a covalent bond involved in stabilising the tertiary structure of a protein.
44
Explain how some medicines can act as competitive inhibitors and describe the properties they need to do this?
Medicines act as competitive inhibitors by being structurally similar to the substrate, allowing them to reversibly occupy the enzyme's active site and prevent the catalysed reaction.
45
HOW TO INCREASE PURITY OF DESIRED PRODUCTS WHEN DISTILLING ?
- Perform repeat distillations at the same temperature.
46