Week 13 Flashcards

1
Q

Polymer

A

Large molecules, composed of many subunits known as monomers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Condensation polymerisation

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Ziegler-Natta catalysts

A

Ti, Zr, Hf or Al based

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

The most common plastics are derived from…

A

Petrochemicals
* Formed by this “addition” polymerisation reaction.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Nylon

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Biopolymers

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Polymers can be biodegradable

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Rotation around C–N bond

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

cis and tran isomers can exist

A

true

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Primary protein structure

A

specific sequence of amino acids in a polypeptide chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
Q

Spike protein on Covid

A

Carbohydrate camouflage on the spike protein makes the virus much more difficult for the human immune system to recognise

26
Q

Many drugs inhibit proteins by

A

mimicking their natural substrate

27
Q

Polar covalents H-bond

A

H is bonded to a very electronegative element (F, O, N)

28
Q

The H-bond is strongest when…

A

the bond angle is 180° as this gets the excess negative charges as far away from each other as possible

29
Q

H-bond “dimer”

A

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
Q

H-bonds and DNA

A

The “double helical” structure of DNA is supported by H-bonds between complementary base pairs on the two intertwining strands

31
Q

H-Bonded Networks

A

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
Q

Unequal numbers of lone pairs and hydrogens in H-Bonded Networks

A

NH3 and HF
* Such H-bond networks affect physical properties like solubility and mixing behaviour, as well as boiling points

33
Q

Concave meniscus

A

Water is more attracted to glass than to itself

34
Q

Convex meniscus

A

Mercury is less attracted to glass than to itself