Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

Bio 181 > Proteins > Flashcards

Proteins Flashcards

You may prefer our related Brainscape-certified flashcards:
Biology 101 flashcards
1
Q

What are the four main elements found in all proteins?

A

nitrogen

carbon

hydrogen

oxygen

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

Some proteins are involved in gene expression and include ___ which assists in synthesizing RNA from DNA. Other proteins are considered defensive proteins and include ___which help destroy microorganisms.

A

RNA Polymerase, antibodies

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

Proteins are made up of chains of ___ acids.

A

amino

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

What are the three major structural components of an amino acid?

A

Side chain (R)

Carboxyl group

Amino group

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

An amino acid may be described as nonpolar, polar uncharged, or polar charged based on the chemical properties of its ___ chain.

A

side (R)

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

The main elements that make up proteins are carbon, hydrogen, __, and __, in addition to small amounts of other elements, like sulfur.

A

nitrogen, oxygen

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

How do the amino acid side chains affect proteins?

A

Amino acid side chains play a critical role in the structure and function of a protein.

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

Cell signaling protein function

A

Allows cells to communicate with each other

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

Metabolic enzyme function

A

Increases the rate of a chemical reaction

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

Transporter function

A

Aids in the movement of solutes across the plasma membrane

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

Motor protein function

A

Initiates movement

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

What are the monomers found in proteins?

A

Amino acids

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

Which of the following accurately describes the chemical structure of a typical amino acid found in a protein?

  • A central carbon is bound to a carbonyl group, an amino group, and two R groups.
  • A central carbon atom is bound to an amino group, carboxyl group, a side chain, and a hydrogen atom.
  • A central carbon is double bonded to both an amino group and a carboxyl group.
A

A central carbon atom is bound to an amino group, carboxyl group, a side chain, and a hydrogen atom.

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

Amino acids are categorized based on:

A

their side chains

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

How can amino acid side chains affect the structure and function of a protein?

A

Amino acid side chains play a role in protein folding.

Amino acid side chains are involved in catalysis at the active site of enzymes.

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

What process is responsible for linking amino acids together to form polypeptides?

A

Dehydration reactions

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

In a peptide bond, which parts of the two amino acids are joined together?

A

The amino group of one amino acid and the carboxyl group of the other

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

When amino acids are linked together they form a large molecule called a(n)

A

polypeptide.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Proteins are made by __ reactions, in which water is removed as amino acids are linked together to form polypeptides.

A

dehydration

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

When a peptide bond is formed, two amino acids are linked between the __ group of one amino acid and the __ group of the other.

A

amino, carboxyl

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

A type of covalent bond called a ___ bond forms between the carboxyl group of one amino acid and the amino group of another amino acid.

A

peptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

A polypeptide is a chain of

A

amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Between what two atoms are peptide bonds located in the backbone of a polypeptide?

A

Carbon and nitrogen

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

A free __ group is found at the N-terminus of a protein, and a free __ group is found at the C-terminus.

A

amino, carboxyl

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

A protein whose highest level of structure is tertiary structure contains:

A

one polypeptide folded into its three-dimensional structure

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

Where are the peptide bonds in a polypeptide located?

A

In the polypeptide backbone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

What functional groups are found at the N-terminus and the C-terminus of a polypeptide?

A

A carboxyl group is at the C-terminus.

An amino group is at the N-terminus.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

What is the primary structure of a protein?

A

The amino acid sequence of a polypeptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

What is the secondary structure of a protein?

A

The repeating pattern of folding between regions

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Match the level of protein organization with the proper description:

primary

A

the linear sequence of amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Match the level of protein organization with the proper description:

secondary

A

repetitive folding patterns such as α helix and β pleated sheet

32
Q

Match the level of protein organization with the proper description:

tertiary

A

the three-dimensional structure of a polypeptide

33
Q

Match the level of protein organization with the proper description:

quaternary

A

two or more interacting polypeptides

34
Q

What are the two types of secondary structure found in proteins?

A

β pleated sheet

α helix

35
Q

Between what two atoms are peptide bonds located in the backbone of a polypeptide?

A

Carbon and nitrogen

36
Q

What type of bond is responsible for the formation of α helices and β pleated sheets?

A

Hydrogen bond

37
Q

The amino acid sequence of a polypeptide is called the ___ structure.

A

primary

38
Q

The ___ structure of a polypeptide is the repeating pattern of folding stabilized by hydrogen bonds.

A

secondary

39
Q

What level of protein organization refers to the three-dimensional shape of a polypeptide that includes all secondary structures and interactions between side chains?

A

Tertiary structure

40
Q

A protein whose highest level of structure is tertiary structure contains:

A

one polypeptide folded into its three-dimensional structure

41
Q

What level of protein structure is stabilized by interactions among the side chains of the polypeptide?

A

Tertiary structure

42
Q

The two basic types of secondary structure are the alpha __ and the beta-pleated __.

A

helix, sheet

43
Q

Proteins that have quaternary structure consist of at least __ polypeptide(s).

A

2

44
Q

The elements of a polypeptide’s secondary structure, the α helix and β pleated sheets are stabilized by ___ bonds.

A

hydrogen

45
Q

What factors contribute to protein-protein interactions?

A

van der Waals effects

hydrogen bonding

hydrophobic effects

ionic bonding

46
Q

Match each bond or interaction with the correct description.

hydrogen bond

A

Bond between partial positive and negative charges on different amino acids

47
Q

Match each bond or interaction with the correct description.

ionic bond

A

Bond between oppositely charged amino acid side chains

48
Q

Match each bond or interaction with the correct description.

disulfide bond

A

Covalent bond between two cysteines

49
Q

Match each bond or interaction with the correct description.

hydrophobic effect

A

Interaction between nonpolar amino acids

50
Q

Match each bond or interaction with the correct description.

van der Waals force

A

Weak, temporary attraction between two atoms

51
Q

The three-dimensional shape of a polypeptide is the ___ structure.

A

tertiary

52
Q

Which levels of protein structure are stabilized by hydrogen bonds?

A

Secondary structure

Quaternary structure

Tertiary structure

53
Q

Interactions among the side chains of amino acids help to stabilize the ___ structure of a polypeptide.

A

teritary

54
Q

What level of protein structure occurs when two or more polypeptides interact with each other to form a functional protein?

A

Quaternary structure

55
Q

What type of bonds can form between positively and negatively charged side chains within a polypeptide?

A

Ionic bonds

56
Q

Interactions between different proteins can be stabilized by four main factors: __ bonds, ionic bonds, __ effect, and van der __ dispersion forces.

A

hydrogen, hydrophobic, waals

57
Q

Which of the following bonds and interactions contribute directly to a protein’s tertiary structure?

  • Peptide bonds
  • Hydrogen bonds
  • Disulfide bonds
  • Hydrophobic effect
  • van der Waals forces
  • Glycosidic bonds
  • Ionic bonds
A

Hydrogen bonds

Disulfide bonds

Hydrophobic effect

van der Waals forces

Ionic bonds

58
Q

Hydrogen bonds can form:

A

within a polypeptide and between different polypeptide chains

59
Q

What level of protein structure is stabilized by interactions among the side chains of the polypeptide?

A

Tertiary structure

60
Q

__ bonds promote protein folding when they form between oppositely-charged side chains of a protein.

A

hydrogen

61
Q

Amino acid side chains that are nonpolar tend to exclude water and contribute to __ effects involved in protein folding.

A

hydrophobic

62
Q

What factors contribute to protein-protein interactions?

A

ionic bonding

hydrophobic effects

hydrogen bonding

van der Waals effects

63
Q

What type of bond can form between the side R groups of two cysteine amino acids to stabilize protein structure?

A

Disulfide bond

64
Q

Which levels of protein structure are stabilized by hydrogen bonds?

A

Quaternary structure

Tertiary structure

Secondary structure

65
Q

Interactions among the side chains of amino acids help to stabilize the ___ structure of a polypeptide.

A

tertiary

66
Q

What functional group is involved in disulfide bridges?

A

Sulfhydryl

67
Q

Hydrophobic effects play a major role in what protein structures?

A

quaternary structure

tertiary structure

68
Q

___ bridges can form between the side chains of two cysteine amino acids.

A

Disulfide

69
Q

A disulfide bond can form between two cysteines located:

A

within the same polypeptide chain or in different polypeptide chains

70
Q

When a protein is unfolded or ______, it is no longer functional.

A

denatured

71
Q

The tertiary structure of a polypeptide is predominantly determined by its __ structure.

A

primary

72
Q

Disulfide bridges are covalent bonds between ___ groups of cysteine side chains.

A

sulfhydryl

73
Q

Amino acid side chains that are nonpolar tend to exclude water and contribute to __ effects involved in protein folding.

A

hydrophobic

74
Q

A disulfide bond between two cysteines in the same polypeptide chain can help to stabilize the ______ structure of a protein.

A

tertiary

75
Q

What happens when a protein is denatured?

A

Its three-dimensional structure is disrupted.

76
Q

What is the main determinant of a protein’s tertiary structure?

A

Its primary structure

77
Q

What functional group is involved in disulfide bridges?

A

Sulfhydryl

Bio 181 (18 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2024 Bold Learning Solutions. Terms and Conditions