E1 Chapter 8: Enzymes and Proteins Flashcards

Exam 1 (42 cards)

1
Q

Protein that aids the selective acceleration of chemical reactions

A

Enzymatic proteins

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

Proteins that provide protection against diseases

A

Defensive proteins

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

Proteins that help to store amino acids

A

Storage Proteins

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

Proteins that aid in the transportation of a substance

A

Transport protein

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

A polymer of amino acids is called

A

A polypeptide

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

A biologically functional molecule made up of one or more polypeptides, each folded and coiled into a 3-D structure

A

Protein

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

An organic molecule with both an amino group and a carboxyl group

A

Amino acid

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

What is the carbon called at the center of an amino acid

A

An alpha carbon

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

The covalent bond between the carboxyl group on one amino acid and the amino group on another, forming a dehydration reaction

A

Peptide Bond

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

A linear chain of amino acids (the protein sequence of amino acids)

A

Primary protein structure

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

Regions stabilized by hydrogen bonds between atoms of the polypeptide backbone

A

Secondary Structures

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

A delicate coil held together by hydrogen bonding between every 4th amino acid

A

Alpha helix

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

Two or more segments of a polypeptide chain laying side-by-side

A

Beta Pleated Sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

3-D shape stabilized by interaction of side chains

A

Tertiary Structures

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Amino acids with hydrophobic side chains usually end up in clusters at the core

A

Hydrophobic interactions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Form where two cystine monomers, which have -SH groups on side, are brought close by folding

A

Disulfide bridges

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

The association of two or more peptides (the overall protein structure that results from the aggregation of polypeptide subunits)

A

Quaternary Structure

18
Q

A process in which protein loses its shape due to the disruption of weak chemical bonds, becoming biologically inactive

19
Q

A macromolecule that acts as a catalyst

20
Q

A chemical agent that speeds up a reaction without being consumed by the reaction

21
Q

Enzymes lower the _______________

A

Activation energy barrier

22
Q

The amount of energy that reactants must absorb before a chemical reaction will start

A

Activation energy

23
Q

The reaction on which an enzyme works

24
Q

A pocket or groove on the surface of an enzyme where catalyzation occurs

25
Are active sites specific or willing to bind many enzymes?
Very specific
26
The change in shape of the active site of an enzyme so it binds more snug to the substrate
Induced fit
27
Does the rate of an enzyme increase with increased or decreased temperature?
Increased
28
If we keep increasing the temperature, what will happen to an enzyme?
It will denaturize and become inactive
29
Why does a higher temp increase reaction rate of an enzyme (to a point)?
Caused by increased speed of substrates colliding with active sites
30
What is the optimal pH value for enzymes?
6-8
31
Any nonprotein molecule or ion that is required for the proper functioning of an enzyme
Cofactor
32
An organic molecule serving as a cofactor is called
coenzyme
33
Reduce the productivity of enzymes by BLOCKING substrates from entering active sites
Competitive inhibitors
34
Reduces the activity of an enzyme by binding to a location remote from the active site
Noncompetitive inhibitor
35
The binding of a regulatory molecule to a protein at one site that affects the function of a protein at a different site
Allosteric regulation of enzymes
36
A method of metabolic control in which the end product of a metabolic pathway acts as an inhibitor of an enzyme within that pathway
Feedback inhibition
37
Products have less energy than reactant (-G)
Exergonic/spontaneous reactions
38
Products have higher energy than reactant (+G)
Endergonic/nonspontaneous reactions
39
Binding of a substrate molecule can stimulate the binding of activity at other active sites
cooperativity
40
Chemical reactions that involve a free energy change
Gibbs Free Energy
41
-G means ___________, while +G means ______________
Spontaneous, nonspontaneous
42
Changing pH disrupts what type of bonds (2)
Hydrogen and Ionic