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Biology 241 > Topic 4 > Flashcards

Topic 4 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

what are enzymes?

A

proteins

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2
Q

what are proteins?

A

polypeptide that is folded into a specific 3D shape

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3
Q

what is a peptide bond?

A

a polar covalent bond between amino acids

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4
Q

characteristics of hydrophobic R groups?

A

many non polar bonds
-inside away from water

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5
Q

characteristics of a hydrophilic R group?

A

side chains with oxygen, nitrogen or charged atoms
-on the outside of an amino acid

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6
Q

what happens when an acid loses a proton at ph7?

A

it becomes negatively charged

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7
Q

what happens when an acid gains a proton at ph7?

A

it becomes positively charged

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8
Q

what is a peptide?

A

polymer of amino acid

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9
Q

what is a polypeptide?

A

polymer of more than 10 amino acids

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10
Q

what is the primary structure of a polypeptide?

A

literal sequence of amino acids (straight line)

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11
Q

what is the secondary a structure of a polypeptide?

A

the primary structure folded into helices
-stabilized by hydrogen bonding by carboxyl groups and amide groups

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12
Q

what is the secondary b structure of a polypeptide?

A

primary sequence is folded into sheets
-stabilized by hydrogen bonds between carboxyl groups and amide groups

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13
Q

what is tertiary structure of a polypeptide?

A

the secondary structure is folded into the 3D shape of a protein
-due to multiple levels of interaction between the R-groups (HB, ionic interactions, Vanderwaals, covalent bonds)

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14
Q

what is quaternary structure of a polypeptide?

A

4 subunits each with tertiary structure

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15
Q

secondary structure of hexokinase?

A

helices, sheets, and turns made by the primary structure

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16
Q

tertiary structure of hexokinase?

A

overall shape of a protein which results from the organisation of secondary structural regions relative to another

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17
Q

what is activation energy?

A

the energy required to get a reaction going

18
Q

how does activation energy work?

A

energy destabilizes the bonds in the reactants which allows the for the formation of the generation of products

19
Q

what is a transition state?

A

the point where bonds in reactants are breaking and bonds of products are forming
-summit of Ea hill

20
Q

what are ways to speed up a chemical reaction?

A

increase temperature
increase concentration of reactants
add a catalyst

21
Q

what are examples of a catalyst?

A

enzyme- protein catalyst
robozyme- RNA catalyst

22
Q

what do catalysts do?

A

decrease activation energy speeding up reaction time

23
Q

what is an active site of an ezyme?

A

a region that interacts with one or more specific substrates

24
Q

what happens when a substrate binds to an enzymes active site?

A

the enzyme changes shape forming an enzyme-substrate complex

25
Q

what does the ES complex do?

A

forces the products into the transition state

26
Q

how does an enzyme get back to how it was originally?

A

it released the products changing the enzymes back into its original shape

27
Q

how do cells regulate enzyme kinetics?

A

by changing the concentration of inhibitors or the concentration of activators

28
Q

what does the rate of an enzyme reaction depend on?

A

the concentration of enzyme and the concentration of substrate

29
Q

what influences how fast a cell can convert substrate into products?

A

the rate of an enzyme reaction

30
Q

what is denaturation?

A

loss of protien structure

31
Q

characteristics of denaturation?

A

partial or complete
reversible or irreversible
caused by heat, pH and non-competitive inhibitors

32
Q

what is inactivation?

A

loss of protein activity

33
Q

characteristics of inactivation?

A

reversible or irreversible
due to denaturation

34
Q

what is a reversible competitive inhibitor?

A

an inhibitor that is chemically like the substrate
-inhibitor noncovalently binds to an enzymes active site and competes with the substrate for binding to the active site
-molecule with the highest concentration outcompetes the other

35
Q

what does competetive inhibition affect?

A

Km increases,
vm is the same

36
Q

what is reversible non-competitive inhibition?

A

inhibitor is unlike the substrate
-inhibitor noncovalently binds to allosteric site
-high concentrations of substrate can’t outcompete inhibitor

37
Q

what does a non-competitive inhibitor affect?

A

decreases Vmax,
Km stays the same

38
Q

what are allosteric enzymes?

A

biochemical pathways that include regulatory enzymes that control the rate of the entire pathway

39
Q

what are allosteric activators?

A

bind to the enzyme which will change shape to a more active form

40
Q

what are allosteric inhibitors?

A

bind to the enzyme which will change shape to a less active form

41
Q

what is feedback inhibition?

A

the final product of a pathway inhibits an enzymes early in the pathway

Biology 241 (12 decks)

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