PROTEINS & ENZYMES Flashcards

(32 cards)

1
Q

what are proteins?

A

proteins are functional units of the cell

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2
Q

what do proteins form?

A

enzymes, structural, transport, storage, signalling, receptors, gene regulation

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3
Q

what links monomers to form polymers?

A

dehydration reaction - forming peptide bonds between 2 amino acid monomers

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4
Q

how many amino acids make up a proteins?

A

20

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5
Q

what determines the structure and function of the protein?

A

side-chain R of the protein

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6
Q

what makes up a protein?

A

variable side chain (R group), Carboxyl group, Hydrogen atom and amino group

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7
Q

how does protein name come about?

A

by the two primary functional groups

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8
Q

how many essential and non-essential amino acid are there?

A

essential : 9 - cannot be synthesized by body

non-essential : 11 - can be synthesized by body

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9
Q

what are the functional group?

A

gives the molecule the properties and are centres of chemical reactivity

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10
Q

what are proteins composed of?

A

C, H, O, N & small amounts of other elements notably sulfur

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11
Q

what are the level of structures?

A

primary, secondary, tertiary, quarternary

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12
Q

what are primary structures?

A

linear order of amino acid joined together by as polypeptide

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13
Q

what are secondary structures?

A

localised folding of linear polypeptide resulting in alpha helix or beta pleated sheet or random loop

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14
Q

what are tertiary structures?

A

3d shape of a protein which closely links to its function

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15
Q

what are quarternary structures?

A

made up of 2 or more subunits of proteins

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16
Q

what are peptides and polypeptide?

A

peptide : 2 or more amino acids linked

polypeptide : chain of amino acids joined by peptide bonds

17
Q

what determines amino acid sequence?

A

the genes - number and sequences of amino acid vary in proteins

18
Q

what happens during secondary structure?

A

chemical and physical interactions causes the polypeptide chains to be folded or pleated into different shapes by hydrogen bonding between amino acids

19
Q

what r group interactions contribute to tertiary structure?

A

hydrogen, ionic, disulphide bonding, hydrophobic interactions and van der waal’s force

20
Q

what happens in quarternary structure?

A

the individual polypeptides join together to form a larger protein - all subunits must be present for protein to function

21
Q

what causes protein to denature?

A

pH or heat cause irreversible change in protein shape

22
Q

what are enzymes?

A

proteins which acts as a catalyst to speed up a chemical reaction

23
Q

what does enzymes have?

A

enzymes have an active site where the substrate binds

24
Q

what are substrates?

A

the molecules that an enzyme work on

25
what can enzymes do?
either break a single structure or join two or more substrate molecules together
26
what are the two mechanism of enzyme action?
lock and key - substrate must be compatible so that enzymes can modify the substrates induced fit hypothesis - enzyme will mold itself to the shape of the molecule once the proper substrates makes contact with the enzyme
27
properties of an enzyme?
- all enzymes are proteins - speed up biochemical reactions - very specific (substrate-specific) - lowers activation energy by lowering energy barrier allowing the reactants to react faster forming the products - not damaged during the reaction - can be reused
28
what do some enzymes require?
cofactors - required in diet of organisms
29
factors that affect the rate of enzyme reaction?
temperature - must hit optimum temp ; high temp breals the disulphide bonds holding the tertiary structure - DENATURED pH - must reach optimum pH (5-9) substrate concentration - directly proportional at the start and no effect nearing the end as all enzymes are working at max. rate enzyme concentration - directly proportional all the way if substrates are in excess enzyme inhibitors - active enzymes is prevented from combing with its substrate
30
what type of enzyme inhibitors are there?
IRREVERSIBLE - Inhibitors are temporarily bound REVERSIBLE - competitive and non-competitive - Inhibitors bind permanently, permanently deactivating the enzyme
31
competitive inhibition
inhibitor competes with the substrate for the active site
32
non-competitive inhibition
inhibitor binds to the allosteric site and alters its shape