Molecules and Proteins Flashcards

1
Q

What is a Macromolecule?

A

large, biologically important molecules inside cells

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2
Q

What are macromolecules generally?

A

sugars, lipids, amino acids,

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3
Q

Is ATP a macromolecule?

A

no ATP is a nucleotide

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4
Q

What are oligosaccharides?

A

3-12 monosaccharides, products of polysaccharide digestion, part of lipid complexes

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5
Q

What causes monosaccharides to form ring structures?

A

often caused by reaction of the aldheyde/ketone group reacting with the hydroxyl group from the same molecule

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6
Q

3 parts of a fatty acid?

A

Methyl group, carbon chain, carboxyl group

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7
Q

Does raising the degree of unsaturation increase or decrease melting point of fatty acids?

A

more unsaturated (more double bonds) causes more kinks, so melting point decreases.

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8
Q

What format are double bonds shown in?

A

(18:1) so for every 18 carbons there is one double bond.

often shown as delta^first time double bond appears.

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9
Q

What are phosphoacylglycerols?

A

derived from phopshatidic acid. formed from fatty acids esterified to glycerol and phosphorylated at C3.

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10
Q

What are Sphingolipids?

A

derived from ceramide. (serine, palmitic acid and another fatty acid)

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11
Q

What are steroids made of?

A

made of cholesterol.

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12
Q

What are steroids used for?

A

emulsify fatty acids to form micelles

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13
Q

Where is cholesterol produced?

A

produced by the liver, absorbed by the gut.

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14
Q

5 points about peptide bonds?

A
very stable.
cleaved by proteolytic enzymes.
Partial C-N bond.
Flexible around C atoms not involved in the bond.
usually have one preferred form.
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15
Q

what forces hold proteins together?

A

Peptide bonds, hydrogen bonds, disulphide bonds, Van der Waals, ionic bonds, hyrophilic/phobic interactions

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16
Q

Secondary structures?

A

Alpha Helix: H-bonds between carbonyl groups and the N-H four amino acids down the chain.
Beta-Sheet: H-bonds between linear regions of polypeptide chains. can be parallel or antiparallel, pleated or not pleated.

17
Q

What are some super-secondary structures?

A

beta-alpha-beta units, helix-turn-helix conformation, zinc fingers.

18
Q

What is and causes tertiary structure?

A

the overall 3D conformation of a protein.
caused be electrostatic, hydrophilic/phobic, H-bonds and covalent interactions.
can change based on pH

19
Q

What is Quartenary structure?

A

3D structure of a protein made of many subunits

20
Q

What are isoenzymes?

A

enzymes who have different structures and sequences but catalyse the same reaction as another

21
Q

What are coenzymes?

A

complex organic structures that help to maximise the repertoire of enzymes function groups.

22
Q

What do activation-transfer coenzymes do?

A

form a covalent bond and are regenerated at the end.

23
Q

what do oxidation-reduction coenzymes do?

A

involved in electron transfer reactions.