Bio Chem Flashcards

(54 cards)

1
Q

What is a chemical reaction?

A

A process that leads to the transformation of one set of chemical substances to another.

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

What are anabolic reactions?

A

Reactions that build larger molecules from smaller ones.

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

What are catabolic reactions?

A

Reactions that break down larger molecules into smaller ones.

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

What is an enzyme?

A

A protein that acts as a catalyst to speed up chemical reactions.

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

What is a pleated sheet?

A

A type of secondary structure in proteins characterized by folded strands.

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

What is an alpha helix?

A

A common secondary structure in proteins formed by a right-handed coil.

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

What are the types of molecular bonds?

A

Ionic bonds, covalent bonds, hydrogen bonds.

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

What is an atom?

A

A single unit made up of neutrons, protons, and electrons.

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

What is an ionic bond?

A

A bond formed by the transfer of electrons from one atom to another.

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

What is a molecule?

A

Groups of 2 or more atoms held together by chemical bonds.

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

What is a covalent bond?

A

A bond formed by the sharing of electrons between atoms.

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

What is a nonpolar molecule?

A

A molecule with equal sharing of electrons.

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

What is a polar molecule?

A

A molecule with unequal sharing of electrons, forming a dipole.

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

What are hydrogen bonds?

A

Weak bonds between a hydrogen atom and an electronegative atom (F, O, or N).

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

What are macromolecules?

A

Large molecules (polymers) formed from the bonding of smaller molecules (monomers).

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

What are the four types of organic macromolecules?

A

Proteins, carbohydrates, lipids, nucleic acids.

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

What is the monomer of proteins?

A

Amino acid.

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

What is the polymer of proteins?

A

Peptide.

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

What type of linkage is found in proteins?

A

Peptide bonds.

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

What is the function of proteins?

A

Structure, transport, defense, storage, enzymes.

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

What is the monomer of carbohydrates?

A

Monosaccharide.

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

What is the polymer of carbohydrates?

A

Polysaccharide.

23
Q

What type of linkage is found in carbohydrates?

A

Glycosidic bonds.

24
Q

What is the function of carbohydrates?

A

Store energy.

25
What are monosaccharides?
Single sugar molecules (e.g., Glucose).
26
What are disaccharides?
Two joined sugar molecules (e.g., Glucose + Fructose = Sucrose).
27
What are polysaccharides?
Polymers of sugar molecules, including starch, glycogen, cellulose, and chitin.
28
What is the primary structure of proteins?
Linear chain sequence of amino acids.
29
What is the secondary structure of proteins?
Local folding of the chain into alpha helices or beta sheets via hydrogen bonding.
30
What is the tertiary structure of proteins?
3D shapes due to noncovalent interactions between R groups.
31
What is the quaternary structure of proteins?
3D protein shape consisting of 2 or more separate peptide chains.
32
What is a Dehydration Reaction?
Links monomers to form polymers, forming H₂O in the process.
33
What is Hydrolysis?
Uses water to break polymers into monomers.
34
What are Lipids?
Nonpolar, hydrophobic molecules.
35
What is the monomer of Lipids?
Hydrocarbons.
36
What is the polymer of Lipids?
Hydrocarbon chain.
37
What type of linkage do Lipids have?
Covalent carbon-carbon.
38
What are the functions of Lipids?
Insulation, energy storage, endocrine signaling, cell structure.
39
What are Triglycerides?
Glycerol + 3 fatty acids. ## Footnote Saturated (single bonds, straight chain) and Unsaturated (double bonds, branched chain).
40
What are Phospholipids?
2 fatty acids + phosphate group attached to glycerol backbone. ## Footnote Amphipathic with polar head, nonpolar tail. Form phospholipid membrane bilayer.
41
What are Steroids?
Three 6-membered rings + one 5-membered ring. ## Footnote E.g., hormones, cholesterol.
42
What are Porphyrins?
4 joined pyrrole rings with a metal center atom. ## Footnote E.g., chlorophyll, hemoglobin.
43
What is the monomer of Nucleic Acids?
Nucleotide.
44
What is the polymer of Nucleic Acids?
Nucleic acid (DNA, RNA).
45
What type of linkage do Nucleic Acids have?
Phosphodiester bond.
46
What is the function of Nucleic Acids?
Encode, express, and store genetic info.
47
What is the structure of a Nucleotide?
Nitrogenous base + 5-C sugar + phosphate group.
48
What distinguishes DNA from RNA?
DNA has -H attached to 2' carbon of the sugar, while RNA has -OH attached to sugar.
49
What are the bases of DNA?
A, T, C, G. ## Footnote Contains deoxyribose sugar and 2 complementary antiparallel (5' to 3') strands of double helix.
50
How do A and T pair in DNA?
A and T pair via 2 H-bonds.
51
How do C and G pair in DNA?
C and G pair via 3 H-bonds.
52
What is Chargaff's Rule?
A & T, and G & C are always present in equal amounts.
53
What is Competitive Inhibition?
A substance that mimics the substrate inhibits enzyme by binding to active site, thus preventing release of substrate. ## Footnote Can be overcome by increasing substrate concentration.
54
What is Noncompetitive Inhibition?
A substance inhibits the enzyme at a secondary location called the allosteric site. ## Footnote Substrate can still bind, but the inhibitor prevents reaction.