WEEK 5 Flashcards

(58 cards)

1
Q

What is the monomer and polymer of a protein?

A

Monomer: Amino acid; Polymer: Polypeptide/protein

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

What are the four parts of an amino acid?

A

Amino group, Carboxyl group, Central carbon, R-group (side chain)

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

What does the R-group determine?

A

The properties and identity of the amino acid

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

How many standard amino acids are there?

A

20

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

What is a peptide?

A

A short chain of amino acids joined by a peptide bond

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

How is a peptide formed?

A

By dehydration synthesis; forms a peptide bond

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

What is a polypeptide?

A

A long chain of amino acids

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

How is a polypeptide different from a protein?

A

A protein is a folded, functional polypeptide

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

What is protein conformation?

A

The 3D shape of a protein

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

Name the four levels of protein structure.

A

Primary, Secondary, Tertiary, Quaternary

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

What is the primary structure of a protein?

A

The sequence of amino acids

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

What is the secondary structure of a protein?

A

Alpha helices or beta-pleated sheets formed by hydrogen bonding

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

What is the tertiary structure of a protein?

A

The overall 3D shape due to R-group interactions

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

What interactions stabilize tertiary structure?

A

Hydrogen bonds, ionic bonds, disulfide bridges, hydrophobic interactions

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

What is the quaternary structure of a protein?

A

The arrangement of multiple polypeptide subunits

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

Do all proteins have quaternary structure?

A

No

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

What is denaturation?

A

Loss of protein structure due to environmental changes

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

How does denaturation affect a protein?

A

It loses its conformation and function

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

What is renaturation?

A

Refolding of a denatured protein under the right conditions

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

List 3 protein functions.

A

Enzymes, structure, transport

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

Globular vs Fibrous protein?

A

Globular: spherical, soluble; Fibrous: long, insoluble

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

What is an enzyme?

A

A protein that speeds up chemical reactions

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

What is a substrate?

A

The molecule an enzyme acts on

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

How are enzymes named?

A

Often based on substrate, ending in “-ase” (e.g., sucrase)

25
How do enzymes speed up reactions?
By lowering activation energy
26
Where does an enzyme bind a substrate?
The active site
27
Can enzymes bind any substrate?
No, they are substrate-specific
28
What is the enzyme-substrate complex?
A temporary complex formed during the reaction
29
What is induced fit?
The enzyme slightly changes shape to fit the substrate
30
Why must enzymes release products?
To repeat the reaction with new substrates
31
How can environment affect enzyme activity?
pH, temperature, and salt levels can alter or denature enzymes
32
What is a cofactor or coenzyme?
Non-protein helpers that assist enzymes
33
What are the monomer and polymer of nucleic acids?
Monomer: Nucleotide; Polymer: Polynucleotide
34
What are the three parts of a nucleotide?
Phosphate, 5-carbon sugar, nitrogenous base
35
How are nucleotides joined?
By phosphodiester bonds
36
What is DNA?
Deoxyribonucleic acid, stores genetic info
37
Name the 4 nitrogenous bases in DNA.
Adenine, Thymine, Cytosine, Guanine
38
Purines vs. Pyrimidines?
Purines (A, G) have 2 rings; Pyrimidines (C, T) have 1 ring
39
How many DNA strands?
Two (double helix)
40
What forms DNA’s backbone?
Sugar and phosphate
41
What forms DNA’s rungs?
Paired nitrogenous bases (A–T, G–C)
42
What does “complementary” DNA mean?
Each base has a specific pair (A–T, G–C)
43
Why is DNA width uniform?
Purines pair with pyrimidines
44
What does “antiparallel” mean in DNA?
Strands run in opposite directions
45
DNA function?
Stores instructions to make proteins
46
Why replicate DNA?
To pass genetic info to new cells
47
What does DNA helicase do?
Unzips DNA at the replication fork
48
What does DNA polymerase do?
Adds new nucleotides during replication
49
What is produced by DNA replication?
Two identical DNA molecules
50
What does "semiconservative" mean?
Each new DNA has one old and one new strand
51
What is RNA?
Ribonucleic acid, single-stranded and used in protein synthesis
52
Name the 4 RNA bases.
Adenine, Uracil, Cytosine, Guanine
53
What base does uracil replace in RNA?
Thymine; Uracil is a pyrimidine
54
4 Differences between DNA and RNA?
RNA: single-stranded, ribose sugar, uracil base, shorter-lived DNA: double-stranded, deoxyribose sugar, thymine base, long-lived
55
What is ATP?
Adenosine triphosphate – energy molecule of the cell
55
Structure of ATP?
Adenine + ribose + 3 phosphate groups
56
ATP's role in the body?
Provides energy by losing a phosphate (forming ADP)
57
What is ADP?
Adenosine diphosphate – can be recharged into ATP