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Biochemistry > Exam 1: Chapter 1-4 > Flashcards

Exam 1: Chapter 1-4 Flashcards

1
Q

What are the characteristics of prokaryotes?

A

-simple cell architecture
-cell wall
-loosely organized genetic information

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2
Q

Define prokaryotes.

A

Unicellular organism without a nucleus. (bacteria & archaea)

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3
Q

What are the characteristics of eukaryotes?

A

-linear DNA organization
-membrane bound structures
-prokaryotic relics

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4
Q

Define eukaryotes.

A

Complex cellular organisms with membrane enclosed organelles that have specialized functions.

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5
Q

Draw the Amine functional group.

A
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6
Q

Draw the alcohol functional group.

A
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7
Q

Draw the thiol functional group.

A
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8
Q

Draw the ether functional group.

A
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9
Q

Draw the aldehyde functional group.

A
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10
Q

Draw the ketone functional group.

A
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11
Q

Draw the carboxylic acid functional group.

A
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12
Q

Draw the ester functional group.

A
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13
Q

Draw the amide functional group.

A
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14
Q

Draw the Imine functional group.

A
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15
Q

Draw the phosphoric acid ester functional group.

A
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16
Q

Draw the diphosphoric acid ester functional group.

A
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17
Q

What is the biological polymer of an amino acid?

A

Polypeptide

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18
Q

What is the biological polymer of a monosaccharides?

A

Polysaccharide

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19
Q

What is the biological polymer of a nucleotides?

A

Nucleic Acid

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20
Q

What biological momomer is this structure?

A

Amino Acid

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21
Q

How do you identify a monosaccharide structure?

A

Sugars have a ~1-1 ratio of carbon: oxygen.

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22
Q

What biological monomer is this structure?

A

Nucleotide

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23
Q

How do identify a lipid structure?

A

Lipids have a high ration of carbon to oxygen/nitrogen/phosphorus.

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24
Q

What are residues?

A

A residue is a monomer that has been incorporated into a polymer.

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25
Q

How are monomers linked together to form different macromolecules?

A

Covalent bonds

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26
Q

What is a polypeptide?

A

A polymer of amino acids linked together by peptide bonds.

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27
Q

What is a protein?

A

A protein is a functional unit consisting of one of more polypeptides.

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28
Q

What kind of bond forms a polysaccharide?

A

Glycosidic bond.

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29
Q

What kind of bond forms nucleic acids?

A

Phosphodiester bond.

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30
Q

What are the major and minor roles of proteins?

A

Major Role:
1. Carry out Metabolic Reactions
2. Support Cellular Structures
Minor Role:
1. Store Energy

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31
Q

What are the major and minor roles of nucleic acids?

A

Major Role:
1. Encode Information
Minor Role:
1. Carry out Metabolic Reactions
2. Support Cellular Structures

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32
Q

What are the major and minor roles of polysaccharides?

A

Major Role:
1. Store Energy
2. Support Cellular Structures
Minor Role:
1. Encode Information

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33
Q

If DeltaG is <0, then…

A

A process is ‘spontaneous’ or ‘favorable’ and products are favored

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34
Q

If DeltaG is >0, then…

A

A process is ‘non-spontaneous’ or ‘unfavorable’ and reactants are favored

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35
Q

What is catabolism?

A

Breaking down larger molecules

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36
Q

What is anabolism?

A

Building complex molecules at the expense of energy.

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37
Q

What is a Hydrogen bond?

A

Hydrogen bonds occur when an H atom in a molecule, bound to O, N, or F is attracted to the lone pairs in another molecule

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38
Q

What is amphipathic molecule?

A

A molecule with both polar & non-polar regions

39
Q

What is the hydrophobic effect?

A

Nonpolar regions cluster together to maximize the entropy of the surrounding water molecules.

40
Q

What is the order of strength of intermolecular forces?

A

Covalent bond > ion-ion > H-bonds > dipole-dipole > London dispersion

41
Q

What is London dispersion forces?

A

At any given moment the electrons may shift more to one side which can influence the molecule next to it.

42
Q

What causes a higher boiling point?

A

Stronger IM forces

43
Q

What is the equation for pOH?

A

pOH = -log [OH]

44
Q

What is the equation for pH using H+ concentration?

A

pH = - log [H+]

45
Q

Does a strong acid have a smaller or big Ka value? pKa value?

A

Strong acids have larger Ka values, and smaller pKa values

46
Q

What happens to [HA] and [A] if pH is < pKa?

A

If pH < pKa than [HA] > [A-]

47
Q

When the pKas are far apart, which one should be used?

A

The pKa value closest to the solution pH

48
Q

When do we consider a buffer to be useful?

A

Within +- 1 pH of its pKa

49
Q

What is acidosis?

A

A condition where blood pH is too low

50
Q

What is alkalosis?

A

A condition where blood pH is too high.

51
Q

How do kidneys help maintain blood pH?

A

Kidneys usually retain HCO3- while eliminating H+ to prevent acidosis

52
Q

How do lungs help maintain blood pH?

A

Lungs breathe faster to raise blood pH and slow breathing to lower blood pH.

53
Q

When should a solution be mostly unprotanated?

A

When pKa is above the pH.

54
Q

What is the general structure of a purine and what are the types?

A

2 rings; Adenine & Guanine

55
Q

What is a nucleotide?

A

A nucleoside with one to three phosphates attached.

55
Q

What is the general structure of a pyrimidine and what are the types?

A

1 ring; Cytosine, Thymine, & Uracil

55
Q

What is a nucleoside?

A

A nitrogenous base attached to a ribose sugar

56
Q

What is the structure of DNA?

A

The two DNA strands are antiparallel and the resulting helix is right-handed.

57
Q

What is the Tm?

A

Tm is the point where half of the DNA is completely separated

58
Q

What increases Tm?

A

Higher GC content

59
Q

Draw Alanine. What are the abbreviations?

A
60
Q

Draw Valine. What are the abbreviations?

A
61
Q

Draw Phenylalanine. What are the abbreviations?

A
62
Q

Draw Tryptophan. What are the abbreviations?

A
63
Q

Draw Leucine. What are the abbreviations?

A
64
Q

Draw Isoleucine. What are the abbreviations?

A
65
Q

Draw Methionine. What are the abbreviations?

A
66
Q

Draw Proline. What are the abbreviations?

A
67
Q

Draw Serine. What are the abbreviations?

A
68
Q

Draw Threonine. What are the abbreviations?

A
69
Q

Draw Tyrosine. What are the abbreviations?

A
70
Q

Draw Cystesine. What are the abbreviations?

A
71
Q

Draw Asparagine. What are the abbreviations?

A
72
Q

Draw Glutamine. What are the abbreviations?

A
73
Q

Draw Histidine. What are the abbreviations?

A
74
Q

Draw Glycine. What are the abbreviations?

A
75
Q

Draw Aspartate. What are the abbreviations?

A
76
Q

Draw Glutamate. What are the abbreviations?

A
77
Q

Draw Lysine. What are the abbreviations?

A
78
Q

Draw Arginine. What are the abbreviations?

A
79
Q

How are amino acids linked together?

A

Peptide bond formation between the N-terminus and C-terminus

80
Q

Which amino acids are hydrophobic?

A

Alanine, Valine, Phenylalanine, Tryptophan, Leucine, Isoleucine, Methionine, Proline

81
Q

What amino acid forms a disulfide bond and through what interaction?

A

Nearby Cys side chains will form a disulfide bond in an oxidizing environment

82
Q

What is Ion-Exchange Chromatography?

A

Separates proteins by containing charged groups that bind to proteins of the opposite charge

83
Q

How are bound proteins eluted in Ion-Exchange Chromatography?

A

Increasing salt concentration or by changing the pH of the buffer to alter the charge of the bound proteins

84
Q

What is Size exclusion chromatography?

A

Separates proteins based on size by using small pores and channels in the beads that separate proteins by size and can vary in range to change the % of proteins that will explore each channel.

85
Q

What is affinity chromatography?

A

Takes advantage of the natural binding properties of a protein or uses an engineered tag in order to make some proteins bind to ligands in a mixture and the rest of the proteins will elute.

86
Q

What is SDS-PAGE?

A

Assesses what is in a protein sample by unfolding proteins and putting them in a gel well in order to measure their size.

87
Q

What is the primary structure of a protein?

A

The sequence of amino acid residues.

88
Q

What is the secondary structure of a protein?

A

The localized conformation of the polypeptide backbone.

89
Q

What is the tertiary structure of a protein?

A

The 3D structure of an entire polypeptide, including all of it’s side chains.

90
Q

What is a quaternary structure of a protein?

A

The spatial arrangement of polypeptide chains in a protein with multiple subunits.

91
Q

What are the different types of regular structures that occur within a protein?

A

Alpha Helices and beta-sheet secondary structure.

92
Q

What is a domain?

A

Regions of a polypeptide that fold independently and have their own functions.

Biochemistry (6 decks)

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