(YELLOW) amino acids , polymers and protiens Flashcards

1
Q

what does a acid do with hydrogens

A

it donates them

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2
Q

what does a base do with hydrogens

A

it accepts them

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3
Q

what does amphoteric mean

A

it means it acts both as a base and a acid

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4
Q

how do you tell if somthing is polar or non-polar

A

Non polar molecules are symmetric with no unshared electrons. Polar molecules are asymmetric, either containing lone pairs of electrons on a central atom or having atoms with different electronegativities bonded.

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5
Q

how do you know if somthing is hydrophobic

A

if it is non-polar

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6
Q

info card read and recite
made by me so its gonna be waffle

also draw how a zwitterion is formed

A

a zwitter ion forms when an amino acid is at its normal state e.g when it is in pH 7 , this is NH3(+)CHRCOO(-) and this is when the amino acid is at its isoelectric point

this is acheived by The -COOH of one molecule will protonate the -NH2 group of an adjacent molecule forming a zwitterion.

this is further proven as zwitter ions show charactisitics of ions :
1) they are white solids which melt or decompose at relativly high tempreatures around 300 oC
2) they are soluable in water

in acidic conditions this amino acid is formed

NH3(+)CHRCOOH

is basic conditions this amino acid is formed :

NH2CHRCOO(-)

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7
Q

what is a isoelectric point and how is it effected

A

an isoelectric point is a point at which a zwitter ion is formed , this is effected by the R group on the amino acid.

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8
Q

At what pH can an amino acid act as a nucleophile? Explain

A

A nucleophile has a lone pair on the N. This only occurs at higher pH values

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9
Q

At what pH can an amino acid act as an acid? Explain

A

at the isoelectric point the -NH3+ group can donate a proton; at lower pH values the -COOH group can also donate a proton

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10
Q

how can amino acids act as buffers

A

acts as a buffer removing added H+ or OH- so minimising the change in pH.

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11
Q

what is the reaction called when two peptides join what does it produce

A

amide link

H2)

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12
Q

how would you heat a dipeptdie to give a zwittwer ion

give conditions and reagents

A

conditions heat under reflux

reagents : 6M HCl followed by addition of water

1) dipeptide splits when adding 1 water and 2 H+
this is done in acidic conditions this gives you

2 x NH3CHRCOOH

2) add more water to remove the pH imbalance to give you

2x NH2CHRCOOH + 2H3O(+)

these amino acids can now be examined

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13
Q

info card read and recite

A

POLYESTERS

Polyesters are formed from the reaction between a dicarboxylic acid and a diol or a diacyl chloride and a diol or even a molecule which has an alcohol group on one side and a carboxylic acid/acid chloride group on the other.

an polyester can form between a acy chloride and hydroxide group

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14
Q

Do you consider that there might be disposal problems with this nylon? Why?

A

Proteases (enzymes) can hydrolyse peptide bonds but not between long hydrocarbon chains. Nylon is hydrolysed by strong acids/alkalis at high temps.

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15
Q

Suggest how the strength of the nylon polymer may be increased

A

extrusion and cold drawing results in polymer chains being aligned (more crystalline regions) in which adjacent chains can form H- bonds with one another. Lone pair on C=O: bonds with d+H –N forming H-bond.

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16
Q

uses of nylon:

A

Ropes, fabrics, fasteners (4-pack fasteners), car tyre cords. Cast into solid shapes for engineering components e.g. bearings, cogs.

17
Q

what are the uses and propertys :
polypropenamide

A

properties :
Polymer can be cross linked forming a water absorbing gel.

uses :
Implant for facial surgery Soft contact lenses Soil conditioners

18
Q

what are the uses and propertys :
polypropenoic acid

A

properties:
Water absorbing gel

uses :
nappies

19
Q

what are the uses and propertys :
polyethenol

A

Properties:
% OH groups determines solubility in water

uses :
Soluble laundry fasteners / bags, liquitab capsules

20
Q
A