Brainscape's Knowledge GenomeTM


Top Flashcards (Certified)
All Flashcards

BIOM 1051 > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

4 types of large biological molecules in body

A
  1. Protein
  2. Carbohydrates
  3. Lipid
  4. Nucleic Acid
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Which one of the four large biological molecules is distinctively different from the others? How?

A

Lipid, all others are polymers

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

Reaction of monomers joining to form polymer

A

Condensation / dehydration

2 mononers join, lose 1 water molecule

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

Reaction of polymer dissembling into monomers

A

Hydrolysis

adding of water, H on one end, OH on another end

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

2 Classes of carbohydrates based on location of carbonyl group (C=O) group

A
  1. Aldoses - carbonyl at end of chain

2. Ketoses - carbonyl in middle of chain

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

Name of bond between monosaccharides

A

Glycosidic linkage

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

Major difference between storage polysaccharides in plant and animal? What is the purpose of that?
(plant: starch, animal: glycogen)

A

Greater level of branching in glycogen –> need multiple enzymes to be broken down –> slow down rate of breaking

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

Monomers of carbohydrates

A

monosaccharide

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

Monomers of protein

A

amino acid

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

pKa of carboxyl group

How would it be changed?

A

pKa: 4
<4: more COOH
>4: more COO-

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

pKa of amino group

How would it be changed?

A

pKa: 9
<9: more NH3+
>9: more NH2

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

Name of the state when 2 ions are present in the amino acid? (NH3+ & COO-) When would it occur?

A

Zwitter ion

4 < pH < 9

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

Name of bond joining amino acids together

A

Peptide bond

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

Word describing amino acids with 4 different substituents

A

chiral

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

Name for isomers that are different in spatial arrangement (mirror images)

A

enantiomers

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

2 models for protein

A
  1. Ribbon Model

2. Space-filling model

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

How many different amino acids are there?

A

20

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

From which end is an amino acid sequence numbered from?

A

amino end (with NH2/NH3+)

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

3 types of secondary structure in protein

A

a helix
B sheet
random coil

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

What is secondary structure stabilized by?

A

hydrogen bonds
(a helix: between nearby residues)
(B sheet: between carbonyl group from one amino acid and amino group from another)

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

What is tertiary structure of protein resulted from?

A

Non-covalent interactions between amino acids and side chains

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

How many polypeptides are there in myoglobin and haemoglobin respectively?

A

myoglobin: 1
haemoglobin: 4

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

What do homologous proteins share? Give an example of homologous proteins.

A

Similar primary, secondary & tertiary structure

e.g. myoglobin & haemoglobin

24
Q

How many polypeptides are in haemoglobin? How are they different?

A

4.

2 alpha chains, 2 Beta chains

25
Where is the mutation in sickle cell disease? What is the mutation?
in Beta chain glutamate --> valine negatively charged --> non-polar
26
What happens in sickle-cell haemoglobin?
Aggregation: mutated deoxyhaemoglobin gets attracted and locked into one another --> form long & insoluble fibres --> greatly reduce capacity to carry oxygen
27
How is insulin activated?
Proteolytic (enzyme) cleavage breaks proinsulin into active insulin with 2 polypeptide chains held together by strong disulfide bonds
28
What is globular protein? And what are its characteristics?
Soluble proteins: 1. hydrophobic amino acids located inside core of protein 2. hydrophillic amino acids on surface of protein
29
Is collagen soluble in water?
No, it is fibrous and insoluble in water.
30
Major function of collagen?
Provide mechanical strength to connective tissue
31
What are the inactive and active forms of collagen called?
inactive: procollagen active: tropocollagen
32
How is collagen activated?
By procollagen peptidase. It breaks the peptide bond linking the loose ends at the amino group terminal and carboxyl group terminal.
33
How many polypeptides are there in collagen? Give an important characteristic of them.
3, they intertwine with each other.
34
What is the structure of collagen called?
triple-helix
35
What is the significance of vitamin C in collagen?
Vitamin C activates prolyl-4-hydroxylase (enzyme) prolyl-4-hydroxylase catalyzes formation of hydroxypoline from proline ring -> form more hydrogen bonds -> strengthening collagen
36
What is a disulfide bond? Between which amino acid would it be formed?
strong covalent bond between 2 sulfides. | Formed between cysteine.
37
What happens to collagen in osteogenesis imperfecta?
glycine (smallest amino acid) at core of the triple-helix is replaced by cysteine --> disrupt helical arrangement and hydrogen bonds --> weakened triple-helix
38
6 steps in collagen biosynthesis:
1. Single strands of polypeptides are formed 2. Hydroxylation (adding of hydroxy group) of proline and lysine side chains 3. Triple-helix is formed 4. Procollagen is converted to tropocollagen by procollagen peptidase 5. Bundles form (associating layers) 6. Cross links form (enzyme attach individual collagen molecules together)
39
3 types of biologically important lipids
1. Fats 2. Phospholipids 3. Steroids
40
What are fats constructed from?
Glycerol and fatty acids
41
How are the fatty acids attached to the glycerol?
Dehydration --> Ester Linkage
42
Another name for fat
triglyceride
43
Functions of fat
1. Energy storage 2. Protect vital organs 3. Insulate body
44
Composition of phospholipid
2 fatty acids and 1 phosphate group attached to a glycerol
45
Where does protein synthesis occur?
In ribosomes
46
What controls protein synthesis?
mRNA
47
Monomer of nucleic acid
nucleotides
48
Polymer of nucleic acid
polynucleotides
49
2 Major types of nitrogenous bases
1. Pyrimidines: 6-membered ring (C, T, U for RNA) | 2. Purines: 6-membered ring fused to a 5-membered ring (G, A)
50
What is the backbone of polynucleotides called? And the appendages?
Sugar-phosphate backbone | Appendages: nitrogenous bases
51
How many polynucleotides are there in DNA?
2 polynucleotides
52
How are the 2 polynucleotides arranged?
in double helix, with backbones running antiparallel to each other
53
Name for spontaneous reaction with net release of energ
Exergonic reaction
54
Name for non-spontaneous reaction with net absorb of energy
Endergonic reaction
55
3 Steps in cellular respiration
1. Glycolysis 2. Citric acid cycle 3. Oxidative phosphorylation

BIOM 1051 (6 decks)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions