Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

Biology > Biology 241 Topic 3 > Flashcards

Biology 241 Topic 3 Flashcards

1
Q

What are most enzymes?

A

Proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What are proteins

A

Polypeptides folded into a 3d shape

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What are ionized amino acids comprised of?

A
  • An amino group
  • A central carbon
  • A R group
  • A carboxl group
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

How are peptide bonds formed?

A

Through a dehydration reaction between 2 amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

What is a dehydration reaction?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are the characteristics of a peptide?

A
  • N-terminal
  • C-terminal
  • R group side chains
  • Backbone
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What do the linkage of Amino Acids create?

A

Peptides

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What makes a hydrophobic R-group?

A

non-polar bonds in the r group side chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What makes a hydrophilic r group?

A

polar bonds in the r group side chain

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How do you identify central carbons?

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is a polypeptide?

A

when more than 10 amino acids join together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is a primary structure?

A

Polypeptide; the sequence of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Was is a quaternary structure?

A

Multiple tertiary structures forming together

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Are most biological reactions slow or fast?

A

Slow

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

What is the energy required for a reaction to proceed?

A

Activation Energy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
What are the 2 types of catalysts?
-Enzymes -Ribosomes
26
What does an enzyme (catalyst) change
It decreases the activation energy
27
What does not change when an enzyme (catalyst) is introduced
The change in energy (G)... the disparity between reactants and products
28
What does an enzymes structure determin?
its function
29
What does every enzyme have?
an active site
30
What is an active site
the location substrates interact with the enzyme
31
What happens when a substrate binds to an active stie? What is this called?
The enzyme changes shape; the enxyme-substrate complex
32
What is the induced fit model?
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
What are the 3 ways an enzyme can change the substrates shape?
- Brings reactants together - Exposes reactant to charged environments - Physically distorts the bonds of substrate
34
What influences enzyme reaction?
-tempurature -substrate concentration -pH -enzyme concentration
35
How is enzyme kinetics regulated?
- enzyme concentration -inhibitors/activators - increased [substrate]
36
Does [substrate] increase or decrease when rate increases and to what extent
increases, until enzyme is saturated
37
What is maximum velocity reffereing too
Maximum saturation level
38
What is denaturization
loss of protein structure
39
What are the characteristics of denaturation
- can be parial or complete - irreversable or reversable - caused by heat or pH
40
What is inactivation
loss of protein activity
41
What are the characteristics inativation
-often due to denaturization - reversible or irreversible
42
What is a competitive inhibitor chemically like
The substrate
43
What way does the comptetitive inhibitor bind to the active site?
Noncovalently
44
True or False: if the competitive inhibitor will always outcompete the substrate
False: it is the one with the highest concentration that will outcompete
45
Which has a higher vmax, no inhibitor or with a competitive inhibitor?
They are equally the same but a competitive inhibitor reaches vmax faster
46
What are the characteristics of a noncompetitive inhibitor
- is not chemically like the substrate - noncovalently bonds at different site than the active site - the inhibitor always outcompetes the substrate
47
What does the vmax look like for a noncompetitive inhibitor
Its vmax is lower
48
What type of structure does an allosteric enzyme have?
Quaternary structure
49
How many active sites does a allosteric enzyme have?
more than one
50
What do allosteric activators do?
Change the enzyme to an active form
51
What do allosteric inhibitors
Change the enzyme to a less active form
52
What is Feedback inhibition
The final product of a pathway inhibits an enzyme early in the pathway
53
What is the name of the girl who I talked to while making these slides
Karis

Biology (5 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions