Week 13 Flashcards

(34 cards)

1
Q

Polymer

A

Large molecules, composed of many subunits known as monomers

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2
Q

Condensation polymerisation

A

Usually involves ejection of a small stable molecule,
* E.g. HCl, CH3OH, H2O

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3
Q

Polymerisation is usually conducted…

A

above the boiling point of the ejected molecule, so it is lost as gas and doesn’t interfere with product

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4
Q

Polymers by addition

A

Addition of alkene monomers and react them with one another and form this growing chain
* Facilitated by a Ziegler-Natta catalyst

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5
Q

Ziegler-Natta catalysts

A

Ti, Zr, Hf or Al based

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6
Q

The most common plastics are derived from…

A

Petrochemicals
* Formed by this “addition” polymerisation reaction.

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7
Q

Nylon

A

Strong synthetic polymer
* The planar amide groups are very polar, so nylon forms multiple hydrogen bonds between adjacent nylon strands
*

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8
Q

Kevlar

A

Rigid/bullet-proof synthetic polymer
High strength from:
* Intermolecular hydrogen bonds formed between the carbonyl groups and in N-H groups.
* Also from aromatic pi-pi stacking interactions that occur between adjacent strands

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9
Q

Biopolymers

A

Polymers found in biological systems
* dd-peptidase: polyamide/peptide
* Cellulose: carbohydrate. The polymer is a polyacetyl.
* DNA: nucleic acid

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10
Q

Polymers can be biodegradable

A

Molecular structure closer to natural biopolymers makes it easier for microorganisms to break them down

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11
Q

Diverse functions of proteins

A
  • structural shape and support
  • mechanical work
  • catalysts
  • regulate body functions
  • protection against disease
  • active in storage and transport
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12
Q

Amino acids condense to form a

A

Peptide (amide) link
* Two amino acids condense to form a di-peptide and three amino acids form a tri-peptide etc.

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13
Q

Rotation around C–N bond

A

Restricted because the C–N bond has some C=N character

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14
Q

cis and tran isomers can exist

A

true

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15
Q

Primary protein structure

A

specific sequence of amino acids in a polypeptide chain

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16
Q

Secondary protein structure

A

Local folded structures that form with the polypeptide chain due to interactions between the atoms of the backbone.
* 𝛼 helix, 𝛽-pleated sheet

17
Q

Tertiary protein structure

A

Interactions between the R groups of the different amino acids that make up the protein (hydrogen bonding, ionic bonding, dipole-dipole interactions and London or dispersion forces) - non-covalent bonds

18
Q

Quaternary protein structure

A

Some proteins are made up of multiple polypeptide chains also known as subunits. When they subunits come together, they give the protein its quaternary structure

19
Q

Acyclovir

A

Derivative of guanine.
Acylovir gets activated by phosphorylation both by viral and host enzymes. The resulting nucleotide becomes incorporated into the newly synthesised viral DNA genome.
* Premature termination of viral DNA synthesis

20
Q

Penicillin

A

If cell walls are improperly made, water flow into the cell causing it to burst. The crosslinking reaction is catalyzed by an enzyme known as transpeptidase.
* Penicillin G, shown here, can mimic the peptide known as the D-alanyl- D-alanine very effectively and inhibit transpeptidase from performing its function.

21
Q

Denaturing

A

Caused by heat, changing pH or chemical reaction
* Usually irreversible: alters biological and physical characteristics (e.g. less soluble)
* Irreversible destruction of both secondary and tertiary structures
* Primary stays the same

22
Q

Random coil

A

What happens to a protein after being denatured

No useful or structural function

23
Q

Covid virus contains many proteins

A

spike, membrane, envelope proteins

24
Q

Polysaccharides

A

carbohydrate polymers that consist of several sugar molecules

25
Spike protein on Covid
**Carbohydrate camouflage** on the spike protein makes the virus much more *difficult* for the human immune system to recognise
26
Many drugs inhibit proteins by
*mimicking* their natural **substrate**
27
Polar covalents H-bond
H is bonded to a very **electronegative** element (**F, O, N**)
28
The H-bond is strongest when...
the bond angle is **180°** as this gets the *excess* **negative** charges as far *away* from each other as possible
29
H-bond “dimer”
Molecules with many O, N or F atoms may have *multiple* H-bond sites. Dimer present: * In the gas phase, When **formic** acid (HCOOH) is in the gas phase (esp. at high pressures * **Long-chain carboxylic acids** in sol.
30
H-bonds and DNA
The “**double helical**” structure of DNA is supported by **H-bonds** between *complementary* **base pairs** on the two intertwining strands
31
H-Bonded Networks
Some molecules that form multiple H-bonds do not “pair up" - form extended one- two- or three-dimensional **networks**. A water molecule can form up to **four** H-bonds through its *two electron lone pairs* and *two d+ hydrogens*. This leads to a **dense**, 3-D network of H-bonded molecules in liquid and solid water
32
Unequal numbers of lone pairs and hydrogens in H-Bonded Networks
NH3 and HF * Such H-bond networks affect **physical** properties like solubility and mixing behaviour, as well as boiling points
33
Concave meniscus
Water is more attracted to glass than to itself
34
Convex meniscus
Mercury is less attracted to glass than to itself