Cells, Small Molecules, Macromolecules, and Proteins Flashcards

(65 cards)

1
Q

Do prokaryotic cells have a nucleus?

A

No

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

Diagram of eukaryotic cell

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

Do eukaryotic cells have a nucleus?

A

Yes

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

Diagram of prokaryotic cell

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

Diagram of animal cell

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

Micro- and macro-molecules

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

Cells contain ___ major families of small organic molecules that are the building blocks for macromolecules

A

Four

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

Diagram showing how macromolecules are composed of subunits

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

Disruption to stable protein conformation

A
  • Proteins and RNAs can fold into stable conformations or structures
  • The folded structure is stabilized by multiple weak, noncovalent intermolecular bonds
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Macromolecules can assemble into macromolecular assemblies

A

Both covalent and non-covalent bonds are required to form a macromolecular assembly such as the ribosome

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

What types of bonds are required to form a macromolecular assembly like a ribosome?

A

Both covalent and non-covalent bonds

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

What are nucleotides?

A

The subunits of DNA and RNA

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

How are phosphates attached to the sugar?

A

By a covalent bond

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

Phosphates in nucleotides

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

Bases in DNA and RNA

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

What are the bases in DNA and RNA?

A

Nitrogen-containing ring compounds, either pyrimidines or purines

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

DNA and RNA contain different sugars

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

Differences between DNA and RNA

A
  • DNA contains the bases G, C, A, T
  • RNA contains the bases G, C, A, U
  • DNA is double-stranded
  • RNA is single-stranded
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

How are nucleotides linked?

A

By phosphodiester bonds

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

Nucleotides are linked by ___ to form ___

A

Phosphodiester bonds to form nucleic acids

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

Diagram of nucleotides in nucleic acids

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

The 5’ end has a ___

A

Free phosphate group

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

The 3’ has a ___

A

Free hydroxyl group

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

Nomenclature and abbreviations

A
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
What is the difference between a nucleoside and a nucleotide?
Nucleoside = base + sugar Nucleotide = base + sugar + phosphate
26
General structure of proteins
27
20 amino acids
28
Each amino acid has a distinct ___
Side chain (R group)
29
Protein nomenclature
- Full name - 3-letter abbreviation - 1-letter code
30
Diagram of amino acids in polypeptide chain
31
What are peptide bonds?
Covalent amide linkages
32
___ and ___ help proteins fold
- Noncovalent bonds - Hydrophobic forces
33
Noncovalent bonds in proteins
34
Hydrophobic forces in proteins
35
Stable 3D conformation of proteins
- Note the variety of shapes and sizes - Both non-covalent and hydrophobic forces stabilize the folded structures
36
Common depictions of protein structure
37
⍺-Helix
- The ⍺-helix is a common polypeptide fold - The N-H of each peptide bond is hydrogen bonded to the C-O bond four amino acids away
38
Bonding in ⍺-helix structure
The N-H of each peptide bond is hydrogen bonded to the C-O bond four amino acids away
39
β-Sheets
- β-sheets are a common feature of polypeptide chains
40
Structure of β-sheets
- β-strands are held together by hydrogen bonds to form a structure called a β-sheet - Note the anti-parallel configuration
41
β-strands are held together by ___ to form a β-sheet
Hydrogen bonds
42
What are the two varieties of β-sheets
Anti-parallel and parallel
43
⍺-helices and b-sheets are elements of the ___ structure
Secondary
44
Separate functional domain of a protein
- Many proteins are composed of separate functional domains - A protein domain is a polypeptide chain that can fold independently
45
Examples of protein domains
46
Can many proteins contain multiple copies of the same protein subunit?
Yes, e.g. dimer and tetramer
47
How are dimers formed?
By interaction between a single, identical binding site on each monomer
48
How are tetramers formed?
By interactions between two non-identical binding sites on each monomer
49
Hemoglobin
- Hemoglobin is an example of how many proteins contain two or more different protein subunits - Hemoglobin contains two copies of each ⍺-globin and β-globin subunits
50
Disulfide bonds
- Covalent bonds that help stabilize a protein fold
51
What kind of bond is a disulfide bond?
Covalent
52
How do proteins bind to other molecules?
- Binding sites allow proteins to interact with specific molecules - The binding of a protein to another molecule - termed ligand - is highly selective
53
Antibodies as an example of how proteins work
- Antibodies are proteins that bind very tightly to their ligands (antigens) - Each antibody molecule is made up of two identical heavy chains and two identical light chains - The two antigen-binding sites are thus identical
54
Specificity of antibody antigen-bind sites
- Each antibody has a distinct antigen-binding site, which recognizes its antigen with high specificity - An individual human can make billions of different antibodies
55
In what ways can antibodies be used as a tool?
- They can be used to purify molecules - They can be used as molecular tags
56
How can antibodies be used to purify molecules?
57
How can antibodies be used as molecular tags? (Biochemical)
58
How can antibodies be used as molecular tags? (Microscopy)
59
Steps of protein purification for studying proteins
- Release the cellular contents - Centrifugation allows the separation of cellular components & separates components on the basis of size and density - Proteins are often separated by column chromatography - Major approaches to determine protein structure: * NMR spectroscopy * Cryo-electron microscopy * X-ray crystallography
60
Releasing cellular contents for protein purification
61
Centrifugation
62
Differential centrifugation
63
Protein separation by column chromatography
64
Three kinds of column chromatography
- Ion-exchange chromatography - Gel-filtration chromatography - Affinity chromatography
65
Major approaches to determining protein structure
Major approaches to determine protein structure: * NMR spectroscopy * Cryo-electron microscopy * X-ray crystallography