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Biology > Biology 241 Topic 3 > Flashcards

Biology 241 Topic 3 Flashcards

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1
Q

What are most enzymes?

A

Proteins

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2
Q

What are proteins

A

Polypeptides folded into a 3d shape

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3
Q

What are ionized amino acids comprised of?

A
  • An amino group
  • A central carbon
  • A R group
  • A carboxl group
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4
Q

How are peptide bonds formed?

A

Through a dehydration reaction between 2 amino acids

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5
Q

What is a dehydration reaction?

A

A reaction that result in the components of water being removed to form a large molecule

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6
Q

What are the characteristics of a peptide?

A
  • N-terminal
  • C-terminal
  • R group side chains
  • Backbone
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7
Q

What do the linkage of Amino Acids create?

A

Peptides

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8
Q

What makes a hydrophobic R-group?

A

non-polar bonds in the r group side chain

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9
Q

What makes a hydrophilic r group?

A

polar bonds in the r group side chain

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10
Q

How do you identify where the peptide bonds are?

A

A Nitrogen (with one hydrogen) is connected with a Carbon (with a double bond to oxygen)

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11
Q

How do you identify central carbons?

A

Connected to a r group, a carbon, a nitrogen, and a hydrogen

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12
Q

What is a polypeptide?

A

when more than 10 amino acids join together

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13
Q

What is a primary structure?

A

Polypeptide; the sequence of amino acids

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14
Q

What is a secondary structure and what 2 shapes do the?

A

The h bonds formed along the backbone, forming helices and sheets

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15
Q

What are helices in a secondary structure

A

Swirl like shape made from a carboxyl group forming a hydrogen bond with an amide 4 amino acids apart

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16
Q

What are sheets in a secondary structure

A

Alternating sticky note shape made from a carboxyl group forming a hydrogen bond wtih an amide in a different part of the polypeptide

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17
Q

Was is a tertiary structure?

A

the overall shape of a protein when the secondary structure folds into a 3d shape from the many different r-group interactions

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18
Q

Was is a quaternary structure?

A

Multiple tertiary structures forming together

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19
Q

What is the difference between homo and hetero in regards to quaternary structure?

A

Homo: the same primary structure (sequence of amino acids) in each subunit (tertiary structure.

Hetero: different primary structures (sequence of amino acids) in each subunit (tertiary structure.

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20
Q

Are most biological reactions slow or fast?

A

Slow

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21
Q

What is the energy required for a reaction to proceed?

A

Activation Energy

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22
Q

What does activation energy do?

A

it destabilizes the bonds which allows the formation of products under ther right conditions

23
Q

What is the “summit”/transition state in an energy graph?

A

the point where reactants break and products form

24
Q

What are the 3 ways to speed up a reaction

A
  1. Increase tempurature
  2. Increase concentration
  3. Add a catlyst
25
Q

What are the 2 types of catalysts?

A

-Enzymes
-Ribosomes

26
Q

What does an enzyme (catalyst) change

A

It decreases the activation energy

27
Q

What does not change when an enzyme (catalyst) is introduced

A

The change in energy (G)… the disparity between reactants and products

28
Q

What does an enzymes structure determin?

A

its function

29
Q

What does every enzyme have?

A

an active site

30
Q

What is an active site

A

the location substrates interact with the enzyme

31
Q

What happens when a substrate binds to an active stie? What is this called?

A

The enzyme changes shape; the enxyme-substrate complex

32
Q

What is the induced fit model?

A

When the enzyme complex forces reactants into the transition state, reducing the need for activation energy. Lastly. the products are released and the enzyme reverts to its orginal shape

33
Q

What are the 3 ways an enzyme can change the substrates shape?

A
  • Brings reactants together
  • Exposes reactant to charged environments
  • Physically distorts the bonds of substrate
34
Q

What influences enzyme reaction?

A

-tempurature
-substrate concentration
-pH
-enzyme concentration

35
Q

How is enzyme kinetics regulated?

A
  • enzyme concentration
    -inhibitors/activators
  • increased [substrate]
36
Q

Does [substrate] increase or decrease when rate increases and to what extent

A

increases, until enzyme is saturated

37
Q

What is maximum velocity reffereing too

A

Maximum saturation level

38
Q

What is denaturization

A

loss of protein structure

39
Q

What are the characteristics of denaturation

A
  • can be parial or complete
  • irreversable or reversable
  • caused by heat or pH
40
Q

What is inactivation

A

loss of protein activity

41
Q

What are the characteristics inativation

A

-often due to denaturization
- reversible or irreversible

42
Q

What is a competitive inhibitor chemically like

A

The substrate

43
Q

What way does the comptetitive inhibitor bind to the active site?

A

Noncovalently

44
Q

True or False: if the competitive inhibitor will always outcompete the substrate

A

False: it is the one with the highest concentration that will outcompete

45
Q

Which has a higher vmax, no inhibitor or with a competitive inhibitor?

A

They are equally the same but a competitive inhibitor reaches vmax faster

46
Q

What are the characteristics of a noncompetitive inhibitor

A
  • is not chemically like the substrate
  • noncovalently bonds at different site than the active site
  • the inhibitor always outcompetes the substrate
47
Q

What does the vmax look like for a noncompetitive inhibitor

A

Its vmax is lower

48
Q

What type of structure does an allosteric enzyme have?

A

Quaternary structure

49
Q

How many active sites does a allosteric enzyme have?

A

more than one

50
Q

What do allosteric activators do?

A

Change the enzyme to an active form

51
Q

What do allosteric inhibitors

A

Change the enzyme to a less active form

52
Q

What is Feedback inhibition

A

The final product of a pathway inhibits an enzyme early in the pathway

53
Q

What is the name of the girl who I talked to while making these slides

A

Karis

Biology (5 decks)

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