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Bio 12 > Biochemistry - Overview > Flashcards

Biochemistry - Overview Flashcards

Chemistry Review, Biomolecules and Enzymes

1
Q

Explain what an atom is and what its composition is?

A
  • An atom is the smallest particle of matter that retains the properties of an element.
  • Protons, neutrons, electrons
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2
Q

What are ions and isotopes?

A
  • ions: an atom that has gained or lost electrons

- isotope: an atom with a different number of neutrons

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3
Q

What is the difference between ionic and covalent bonding?

A

ionic: transfer of electrons between a non-metal and a metal
covalent: sharing of electrons between non-metals.

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4
Q

What causes a polar molecule? what does a polar covalent bond create?

A
  • un-equal sharing of electrons

- dipole

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5
Q

What is pH?

A

the concentration of hydrogen ions in a substance

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6
Q

What are the intramolecular forces of water? intermolecular?

A
  • intra: polar covalent bondign (dipole)

- inter: H-bonging

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7
Q

Explain how water is considered the universal solvent. How is this important to our bodies? example.

A
  • it’s polar so it will dissolve other polar substances
  • ionic and other polar covalent molecules
  • not non-polar substances.
  • transports in our bodies, facilitates reactions
  • water will mix with salt but not oil
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8
Q

Explain how water has a high heat capacity/vaporization point. How is this important to our bodies? example.

A
  • due to h-bonds it takes a lot of energy to change water’s state.
  • moderates temp in our bodies, buffers internal temp changes
  • moderates climate, the balloon experiment
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9
Q

Explain how water is cohesive/adhesive. How is this important to our bodies? example.

A
  • Co: water molecules stick together because of h-bonds.
  • Ad: bond to other surfaces, polarity
  • transportation system and lubricants
  • water on a penny
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10
Q

Explain how water has high surface tension. How is this important to our bodies? example.

A
  • h-bonds hold together well

- not as important in our bodies but in nature, organisms use this to move across the water.

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11
Q

Explain how water is less dense in solid-state. How is this important to our bodies? example.

A
  • h-bonds cause frozen molecules to arrange in a crystalline structure
  • not as important in our bodies but in nature, insulates semi-frozen lake and prevents sudden temp changes
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12
Q

What causes a neutral pH?

A

equal numbers of hydride ions and hydroxide ions

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13
Q

What type of bond forms between:

1) metal and a non-metal element
2) two inorganic non-metal elements
3) the hydrogen atoms and the oxygen atom in a single water molecule
4) the hydrogen atoms and the oxygen atoms of adjacent water molecules

A

1) ionic
2) covalent
3) polar covalent (intra)
4) h-bond (inter)

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14
Q

What characteristic of water accounts for its polarity?

A

un-equal sharing of electrons

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15
Q

The polarity of water accounts for what characteristic?

A

its ability to act as a solvent.

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16
Q

Which organelle within the cell is responsible for water storage?

A

vacuoles

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17
Q

In what organelle do hydrolytic reactions occur?

A

lysosomes

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18
Q

What characteristics make carbon unique?

A
  • four bonding pairs
  • able to form strong bonds with itself
  • can form long chains and rings
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19
Q

What are the elements of life?

A

CHNOPS

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20
Q

What are monomers? Polymers?

A

building blocks

lager molecules made of monomers.

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21
Q

What is Hydrolysis? what does it require?

A

water is added to break the covalent bonds of polymers

- requires hydrolytic enzymes

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22
Q

What is Dehydration Synthesis?

A

loss of water to bond monomers into polymers.

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23
Q

Define hydrophilic and hydrophobic?

A

illic: water-loving
obic: water-hating

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24
Q

What is a Carbohydrate?

A

a compound made of carbon, hydrogen, oxygen

n(C)2n(H)n(O)

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25
Q

What is the monomer of a carbohydrate?

A

monosaccharide

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26
Q

What is the difference between glucose and galactose?

A

OH and H branches are fliped

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27
Q

What specific carb is vital for energy in our bodies? Where in our cells is it converted to energy?

A

Glucose, Mitochondria

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28
Q

What are the four functions of a carb?

A

1) energy production
2) energy storage
3) structural role
4) cell to cell recognition

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29
Q

What is excess glucose stored as in our body, where?

A

glycogen in our liver

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30
Q

What are the polymers of carbs called what are the three types?

A

polysaccharides

  • Glycogen
  • Starch
  • Cellulose
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31
Q

What is Glycogen?

A
  • highly branched polymer of glucose
  • animal-based
  • back up energy
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32
Q

What is Starch?

A
  • slightly branched polymer of glucose
  • plants stored energy
  • slightly branched
  • plant-based
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33
Q

What is Cellulose?

A
  • un-branched plant carb
  • humans can’t digest it
  • most prominent carb on earth
34
Q

What are Lipids composed of?

A

Carbon Oxygen and Hydrogen

35
Q

What are the three types of Lipids?

A

1) Fats and Oils - Triglycerides
2) Phospholipids
3) Steroids

36
Q

What are the functions of Lipids?

A
  • Structure
  • Energy (long term)
  • Cushioning
  • Insulation (myelin)
  • Chemical messengers (hormones)
37
Q

What is the structure of Triglycerides?

A

one glycerol and three fatty acids

38
Q

What is the structure of a Phospholipid?

A

one glycerol + two fatty acids and a phosphate group

39
Q

What is the structure of a Steroid?

A

four-carbon ring structure

40
Q

Saturated vs Unsaturated fatty acids.

A
  • animal vs plant
  • single bonds vs some double bonds
  • solid at room temp vs liquid
  • full of hydrogen vs not at max capacity
41
Q

What are Triglycerides important for?

A

Energy storage

42
Q

Do Tyglicerides have a charge?

A

No, they are hydrophobic

43
Q

What are Phospholipids important for?

A

cell membrane bi-layer

44
Q

Do Phospholipids have a charge? Explain.

A

Yes Hydrophilic head hydrophobic tails

45
Q

What is bile an example of?

A

Emulsification breaking fats into small pieces

46
Q

What is Cholesterol important for?

A
  • component of the cell membrane (structure + fluidity)

- a building block for many steroids

47
Q

What is the comparison between LDL and HDL?

A

LDL - takes cholesterol into arteries
HDL - mokes cholesterol out of your body

HDL is better for you

48
Q

What is the purpose of Nucleic Acids?

A
  • store and transfer genetic information

- store energy and ATP

49
Q

What is the monomer of a Nucleic Acid?

A

nucleotide

50
Q

Explain the stricture of a Nucleotide?

A

phosphate group attached to a 5-carbon sugar attached to a nitrogen-containing base.

circle bond bend bond pentagon bond hexagon and maybe an additional pentagon

51
Q

What is ATP? (5)

A
  • Adenosine Triphosphate
  • type of nucleotide
  • molecule of energy
  • formed in mitochondria in cellular resperation
  • consists of an adenosine group(hexagon + pentagon) bonded to a ribose sugar bonded to three consecutive phosphate groups
52
Q

What are the two Polymers of Nucleic Acids? what differentiates them in structure.

A
  • Deoxyribonucleic Acid (DNA)
  • Ribonucleic Acid (RNA)

their sugars

53
Q

What is does a sugar-phosphate backbone refer to?

A

the sugar + phosphate groups of the nucleotides bonding together via covalent bonds.

(third Carbon to below phosphate)

54
Q

What is the difference between Purines and Pyrimidines?

A

Pur: double ring structure
Pyr: singe ring structure

55
Q

What are the Purines and the Pyrimidines?

A

Pur: Adenine, Guanine
Pyr: Thymine or Uracil, Cytosine

56
Q

What are the important characteristics of DNA? (4)

A
  • antiparallel and complementary pairing
  • contains genetic info, controls cell’s activities
  • double helix
  • Thymine not Uracil
57
Q

What are the important characteristics of RNA? (3)

A
  • single helix
  • Uracil not Thymine
  • helps with protein synthesis
58
Q

What are the three types of RNA?

A
  • messenger
  • ribosonal
  • transfer
59
Q

What percent of the dry weight of living organisms is proteins?

A

50%

60
Q

What are the functions of Proteins? (5)

A
  • structure (cell membranes, fingernails)
  • transport (hemoglobin)
  • regulatory (protein hormones)
  • catalysis (enzymes)
  • locomotion (muscles)
61
Q

What is the monomer of a protein?

A

Amino Acid

62
Q

What is the structure of an amino acid?

A

H(2)N-C(HR)-COOH

amine group - remainder - acid group

63
Q

What type of bond, bonds two amino acids together?

A

pepetide bond

64
Q

What is the name of two amino acids bonded together?

A

dipeptide

65
Q

What is the name of the polymer of a protein?

A

polypeptide

66
Q

What is the level of protein orgainization where the orgiginal organization of amino acids and function of the protein come from?

A

primary

67
Q

What level of organization do proteins get a function?

A

tertiary

68
Q

What can cause denaturation of proteins? (4)

A
  • heavy metals
  • high temperatures
  • changes in ph
  • high salt concentration
69
Q

What woould change the primary level or organization in a protein?

A

hydrolysis

70
Q

What does denaturation of a protein mean?

A
  • interfere with the bonding in the secondary and tertiary structures
  • destroyed shape of protein
71
Q

Explain the types of bonds within the primary to quantanary levels of structure? (4)

A

1) covalent bonds aka peptide bonds
2) peptide bonds, h-bonds between R groups
3) peptide bonds, h-bonds, ionic bonds, disulfate bridges between R groups
4) bonding bwtween tow or more tertiary level proteins.

72
Q

What is metaboliam?

A

the sum of all chemical reactions in the body

73
Q

What does anabolic mean? catobolic?

A

anabolic: to buil up or put together
catabolic: to break down to tear apart

74
Q

What is a metabolic pathway?

A

a series of linked chemical reactions

75
Q

What are two ways to stop a metoblic pathway?

A

remove an enzyme or remove the first/original reactiant

76
Q

What are enzymes? What is their funciton?

A

they are proteins that catalyse the rae of a chemical reaction

they lower teh required activation energy in a reation

77
Q

In an enzyme catalysed reaction, what name do we give reactants?

A

substrates

78
Q

How can enzymes be denaturated?

A
  • extreme temp changes
  • ph changes
  • heavy meatals
79
Q

Describe the difference between the lock and key model and the induced fit model.

A

L+K is a highly regulated pairing of substrates and aenzymes. The substrate will fit exactly into on on the enzyme. But for the IF model the enzyme molds slightly to acomodate the substrate(s).

80
Q

Why do we only need a small amount of a particular enzyme in a cell?

A

the enzymes are recyceled.

81
Q

What are the two types of inhibitors? Explain?

A

1) competitive - physically blocks the active site on the enzyme.
2) changes the shape of the active site, usually heavy metals like Lead and Mercury.

82
Q

What is a Cofactor?

A

they donate energy-rich electrons to the reaction to help (superpower) the enzyme, aka coenzymes and vitamins

Bio 12 (10 decks)

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