Chemistry of Life Flashcards

1
Q

Fundamentals of Molecular Medicine

A
  1. DNA Synthesis and Function
  2. RNA Synthesis and Function
  3. Protein Synthesis and Function
  4. Membrane channels & Ionic Movements
  5. Receptors and Signal Transduction
  6. Genetic Past & Genetic Future
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2
Q

Fundamental of Cellular Medicine

A
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3
Q

Matter

Proteins

Nucleic Acids

Phospholipids

ATP

A
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4
Q

Electrons

A
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5
Q

Ionizing Radiation

A
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6
Q

Another form of Ionizing Radiation

A
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7
Q

Ionizing Radation in Medicine

A
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8
Q

Ultraviolet Radiation

Effect of UV Radiation

A
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9
Q

How much is one mole?

A
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10
Q

What is one molar?

A
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11
Q

Electrons, Protons, and Atomic Weight

A
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12
Q

One Molar of NaCl

A
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13
Q

0.14 molar NaCl

A
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14
Q

Normal Serum Electrolyte Reference Ranges “normal ranges”

A
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15
Q

mmols vs. mEq

A
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16
Q

What unit are Albumin Levels?

A
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17
Q

What unit to describe calcium levels

A
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18
Q

What unit describes glucose levels

A
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19
Q

What 2 units describes ethanol levels?

A
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20
Q

Equation for pH

A
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21
Q

Describe the significance of pH=0 and pH=14

A
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22
Q

Describe the basicitiy and acidity of common household items.

Describe in words what pH means.

A
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23
Q

What are the elements that comprise the human body?

A
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24
Q

What elements lead to pathology in humans?

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25
Q

What elements are used to treat disease?

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26
Q

Where are proteins mainly found?

27
Q

What are the functions of proteins and what tasks do they perform in the human body?

28
Q

Variation in size of proteins

29
Q

Examples of Different Proteins related to their tasks

30
Q

Enzyme Hexokinase

31
Q

Transcription Factor

32
Q

Structural Classifications of Proteins

33
Q

Secondary Structure

34
Q

Interactions comprising secondary structure

35
Q

Primary structure. Which terminus comes first?

A

Amino acids

36
Q

Primary structure is comprised of which atoms?

37
Q

How are amino acids classified/distinguished?

38
Q

Draw out Amino-Terminus and Carboxy Terminus and their correct order.

39
Q

Which components join together to form proteins?

What is this process called and what drives it?

40
Q

Relative to the protein where do many hydrophobic amino acids find themselves?

41
Q

Role of hydrophobic amino acids

42
Q

What is cysteine and what is its role/function?

43
Q

Draw out Cysteine forming a Disulfide bond

44
Q

What is the charge of Aspartate?

45
Q

What is the charge of lysine?

46
Q

What type of interaction do amino acids like aspartate and lysine exhibit?

47
Q

Draw serine out and what functional group does it contain?

48
Q

Explain the process and significance of phosphorylation.

49
Q

What is the significance of kinases and phosphatases? What are the outcomes of their activity?

50
Q

What are catalysts?

What is their role regarding the transition state?

Where are they generally located?

51
Q

What levels of protein structure do enzymes often exhibit?

52
Q

Where does a substrate bind?

53
Q

Describe the induced fit model and its subsequent feedback inhibition

54
Q

Explain competitive product inhibition

55
Q

Allosteric site and allosteric activator/inhibitor

56
Q

Multiple levels of regulation in metabolic pathways

57
Q

Draw a model of allosteric activation/inhibition

58
Q

What is a co-factor?

59
Q

What elements make up enzymes?

60
Q

Coenzymes

61
Q

Coenzymes in telomerase formation

62
Q

What are nucleic acids and where do they generally make proteins?

63
Q

Role of Phospholipids

64
Q

Role of ATP