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WBiology > Biochemistry > Flashcards

Biochemistry Flashcards

1
Q

Biochemistry: def

A

study of chemistry in living things

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2
Q

What are the 2 types of substances?

A
  1. Inorganic
    - Molecule does not contain C + CO2
  2. Organic
    - Molecule contains C
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3
Q

What are the types of organic compounds?

A
  • Protein
  • Lipids
  • Carbohydrates
  • Nucleic Acid (DNA)
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4
Q

Molecular Formula: def

A

shows type of elements and number of atoms

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5
Q

Structural Formula: def

A

shows arrangement of atoms in space

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6
Q

Monomer: def

A

identical or similar small sub-units

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7
Q

Polymer: def

A

larger molecules made by joining monomers

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8
Q

What are some strong bonds and why are they important in living organisms?

A

Covalent bonds: sharing of a pair of electrons between 2 atoms to join atoms in a molecule together

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9
Q

What are some weak bonds?

A
  1. Hydrogen Bond: weak attractions between slightly negative end of the one molecule (O, N) and a slightly positive H in another molecule (dictated by dotted lines)
  2. Hydrophobic Interaction: association of hydrophobic molecules or parts of molecules to each other, because they are excluded from water
  3. London’s Force: random movement of electrons causes momentary slight positive and negative charges in atoms causing attraction
  4. Ionic Bond: electrostatic attraction of oppositely charged ions
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10
Q

Why is water crucial for life?

A
  • Has a high specific heat capacity
  • Acts as a solvent by surrounding ions or polar molecules
  • As the particles slow down and get closer, they repel
  • Sticks together (cohesion)
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11
Q

Which types of molecule are hydrophilic?

A
  1. Ionic compounds
    - Dissociate into ions
    - Ion-dipole attraction
  2. Polar covalent compounds
    - Anything charged (sugars, alcohols)
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12
Q

Which types of molecules are hydrophobic?

A
  1. Large nonpolar molecules
    - Fats and oils
  2. Smaller nonpolar molecules are only slightly soluble in water
    - Oxygen gas and carbon dioxide gas
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13
Q

What happens when water autoionizes?

A

One water molecule transfers an H+ ion to the other, resulting in OH (aq) and H₃O (aq)

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14
Q

What is an acid?

A
  • Dissociates to release H+
  • Increases cocnentration of H3O
  • Sour
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15
Q

What is a base?

A
  • Dissociates to form OH
  • Increases the concentration of OH
  • Bitter
  • Slippery
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16
Q

What is an indicator and what are some examples?

A

A substance that changes colour as the concentration of H and OH changes

  • Litmus paper
  • Phenophthalein
  • Universal indicator
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17
Q

What do acid-base buffers do?

A
  • Resists change in pH when acid or base is added
  • Absorbs protons from acids
  • Releases protons upon the addition of a base
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18
Q

What are some examples of acid-base buffers?

A
  • The pH of blood is 7.4
  • eg. Bicarbonate (HCO3) buffers the pH levels in order to make sure the body functions properly
  • eg. Protein
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19
Q

What is the basic structure of an organic molecule?

A
  • Carbon backbone (R) with functional groups attached (CₓHᵧ)

- Carbon has 4 valence electrons so can form chains, branch chains, and rings

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20
Q

Functional Group: OH

A

Hydroxyl
- Alcohols (eg. Ethanol)

R-O-H (bent)

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21
Q

Functional Group: O=C

A

Carbonyl
- Aldehyde/Ketone (eg. Formaldehyde, acetone)

C; -R, =O, -H
C; -R, =O, -R

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22
Q

Functional Group: COOH

A

Carboxyl
- Organic Acids (eg. Citric Acid)

C; -R, -OH, =O

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23
Q

Functional Group: NH2

A

Amino
- Amines (eg. Amino Acids)

N; -R, -H, -H

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24
Q

Functional Group: SH

A

Sulfhydryl
- Thiols

R - S - H (bent)

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25
Q

Functional Group: PO4

A

Phosphate
- Phospho (eg. Phospholipids, nucleotides)

O; -R, -P-O negative, =O, -O negative

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26
Q

Is ionic bonding weak?

A

Yes, in living organisms as the ions just dissociate

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27
Q

What can perform the condensation/hydrolysis reaction?

Also, what to remember to draw?

A
  • Hydroxyl and Carboxyl
  • Phosphate in low pHs can pick up H
  • Hydroxyl and Hydroxyl
  • Carboxyl and Carboxyl
  • Amino and Carboxyl
  • Amino and Hydroxyl

DRAW WATER!

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28
Q

What is a dehydration synthesis reaction?

A

Formation of covalent bond through loss of water molecule used to join monomers

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29
Q

What is hydrolysis?

A

Addition of water to break covalent bond between monomers

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30
Q

When do linkages form?

A

Formed when 2 functional groups undergo a condensation reaction

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31
Q

Why are linkages important?

A

Links units of organic molecules into macromolecules that make up living organisms

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32
Q

Ether: functional groups, molecules found in

A
  • Hydroxyl and Hydroxyl

- Ethers

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33
Q

Glycosidic: functional groups, molecules found in

A
  • Hydroxyl and Hydroxyl (sugars)

- Dissacharides + Polysaccharides

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34
Q

Ester: functional groups, molecules found in

A
  • Hydroxyl and Carboxyl

- Fatty Acids + Phospholipids

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35
Q

Phosphodiester: functional groups, molecules found in

A
  • Hydroxyl and Phosphate

- Nucleic Acids + Phospholipids

36
Q

Peptide: functional groups, molecules found in

A
  • Carboxyl and Amino

- Proteins

37
Q

What is the structure of carbohydrates?

A
  • C, H, O
  • Ratio of 2 H: 1 O
  • Hydroxyl and Carbonyl (aldose sugar at end, ketose sugar in the middle)
38
Q

What are the functions of carbohydrates (3)?

A
  • Source of energy for cells
  • Cell identity marker on membranes
  • Form cell walls in plants or exoskeletons in anthropods
39
Q

What is a monosaccharide (carb)?

A
  • Single unit sugars

- Those with 5+ carbons form ring structures when dissolved in water

40
Q

What are some examples of monosaccharides?

A

Ribose (RNA), deoxyribose (DNA), glucose (energy, structure), ribulose (photosynthesis)

41
Q

What are glucose’s 2 isomers?

A

Fructose, galactose

42
Q

What is a dissaccharide (carb)?

A
  • 2 unit sugars

- Two monosaccharides joined in a dehydration synthesis reaction, forming glucosidic linkage

43
Q

How do you make maltose, sucrose, and lactose?

A

Glucose + Glucose = Maltose + water (alpha 1,4)

Glucose + Fructose = Sucrose + water (alpha)

Glucose + Galactose = Lactose + water (beta 1,4)

44
Q

What is a polysaccharide (carb)?

A
  • Many units of sugars (polymer) joined in a dehydration synthesis reaction, forming glycosidic linkage
  • Polar, hydrophillic
  • Can’t dissolve easily
45
Q

How do animals and plants access the glucose from polysaccharides?

A

Animals and plants possess amylase which breaks the alpha 1,4 glucosidic linkages from end of molecule + a second that breaks the alpha 1,6 glycosidic linkages allowing the glucose to be used as fuel

46
Q

What are examples of polysaccharides?

A 
Amylose (starch)
Amylopectin (starch)
Glycogen
Cellulose
Chitin
47
Q

What is Amylose?

A
  • Straight chain polymer
  • Alpha gluclose in alpha 1,4 glycosidic linkage
  • In plants
48
Q

What is Amylopectin?

A
  • Branched chain polymer
  • Alpha glucose in alpha 1,4 and 1,6 glycosidic linkages
  • In plants
49
Q

What is Glycogen?

A
  • Highly branched chain polymer
  • Alpha glucose in alpha 1,4 and 1,6 glycosidic linkages
  • In animals
50
Q

How do you test for carbohydrates?

A
  • Starch turned black in the presence of iodine solution

- Sugar turns red in the presence of Benedict’s solution when heated

51
Q

What is the basic structure of a lipid?

A
  • Not a polymer
  • Consist of C, H, O
  • Lots of H: little O
  • Hydrophobic
52
Q

What are some examples of a lipid?

A

Fats, oils, wax, hormones, cholestorol

53
Q

Which of the macromolecules are polymers?

A

All but lipids

54
Q

Tell me about saturated fatty acids; their structure, their source, and their room temperature

A
  • Carboxyl + hydrocarbon in ester linkage
  • Animal sources
  • Only single bonds
  • Straight so can stack and form many London forces
  • Solid in room temperature
55
Q

Tell me about UNsaturated fatty acids; their structure, their source, and their room temperature

A
  • Carboxyl + hydrocarbon in ester linkage
  • Plant sources (and fish oil)
  • C=C causes a bend in C chain so they don’t stack closely
  • Few London forces between molecules because of less interaction bt molecules
  • Liquid at room temp
56
Q

What do fats do, and how are they made?

A
  • Involved in energy storage

- Dehydration synthesis reaction between a glycerol molecule and a fatty acid

57
Q

What is the structure of a triglyceride?

A

Dehydration synthesis between glycerol and 3 fatty acids

58
Q

What is a glycerol?

A

Alcohol with hydroxyl

59
Q

What is the structure and function of a phospholipid?

A

2 fatty acids in ester linkage to hydroxyl + phosphate group attached to nitrogen group in phosphodiester linkage to hydroxyl

It is amphipathic and crucial for cell membranes

60
Q

What is the structure, some examples, and function of a steroid?

A
  • 4 carbon rings in their structure, not dehydration synthesis
  • eg. Steroid hormones, cholesterol
  • Crucial for cell membrane and hormones
61
Q

How does soap work?

A

Hydrophobic end faces grease to emulsify it

Hydrophillic end faces out and washes away water

62
Q

How do you test for fats?

A

Paper becomes translucent

63
Q

What is the structure of proteins?

A

Monomer amino acids joined in peptide linkage via dehydration synthesis to form peptides

Composed of amino group and carboxyl attached to central carbon

Distinguished between R groups

64
Q

What are the different groups of amino acids?

A
  • Electrically charged: form ionic bonds
  • Polar: form H bonds
  • Nonpolar: hydrophobic interaction hold R groups together
  • Thiol Containing: Sulfhydryl groups form disulfide bridge with one another
65
Q

What is the primary level of proteins?

A

Polypeptide chain of amino acids linked by peptide linkages

66
Q

What is the interaction in the primary level of proteins?

A

Covalent peptide linkage between amino and carboxyl

Strongest

67
Q

What is the secondary level of proteins?

A

1+ polypeptide chains individually coiled into an alpha helix or beta sheet

68
Q

What is the tertiary level of proteins?

A

Folding of coiled polypeptin chain to form globular protein

69
Q

What is the quaternary level of proteins?

A

Assembly of 2+ folded sub-units (polypeptide) with beta and alpha chains

70
Q

What is the interaction in the secondary level of proteins?

A

H bonding between polar amino acids

71
Q

What is the interaction in the tertiary level of proteins?

A
  • Hydrophilic and hydrophobic R groups (dipole-dipole, London forces)
  • H bonding
  • Disulfide bridges (covalent)
  • Charged R groups (forming ionic bonds)
72
Q

What is the interaction in the quaternary level of proteins?

A
  • Hydrophobic interactions
  • H bonding
  • R group interaction
  • London forces

Weak bonds, easiest to disrupt

73
Q

How does salt solutions cause protein denaturation?

A

disrupt ionic and H bonds (charges)

74
Q

How does heat cause protein denaturation?

A

increased motion of particles disrupts weak bonds maintaining shape except for disulfide bridge

75
Q

How do organic solvents cause protein denaturation?

A

nonpolar R groups are soluble in the solvent which will cause the protein to invert (hydrophillic and hydrophobic sides switch)

76
Q

How do changes in pH cause protein denaturation?

A

disrupt ionic and H bonds (H+ ions)

77
Q

What are the functions of protein (8)?

A
  1. Transport of O₂ (hemoglobin)
    Needs iron ion as cofactor in its structure
  2. Immune System (antibodies)
  3. Enzymes - catalyze reactions
  4. Structural (hair, nails, antlers, hooves)
  5. Contractile Proteins - movement
  6. Cell Signals - protein hormones (insulin)
  7. Membrane Transport - carrier proteins
  8. Energy Storage - during starvation
78
Q

How do you test for proteins?

A

When Biuret’s solution is added to a protein, the solution turns violet

79
Q

What are the 2 types of nucleic acid?

A
  1. RNA (polymer)

2. DNA (polymer)

80
Q

How are nucleic acids formed?

A

Joining nucleotides in dehydration synthesis reactions

81
Q

What are the functions of nucleic acid (2)?

A
  • Genetic information of the cell

- Involved in protein synthesis

82
Q

What kinds of molecules are the functional groups and how polar are they?

A

All polar or ionic

Phosphate > Carboxyl > Amino > Hydroxyl > Carbonyl > Sulfhydryl

83
Q

What are the 4 types of macromolecules?

A
  1. Proteins
  2. Polysaccharides
  3. Lipids
  4. Nucleic Acids
84
Q

What are the most abundant elements in the body and their electronegativities?

A

C, H (low EN)

O, N (high EN)

85
Q

What is chitin and cellulose?

A

Beta glucose units joined in a beta 1,4 glycosidic linkage

WBiology (8 decks)

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