Chemistry of Life Flashcards Preview

Fundamentals of Molecular Medicine > Chemistry of Life > Flashcards

Flashcards in Chemistry of Life Deck (64)
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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
2
Q

Fundamental of Cellular Medicine

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3
Q

Matter

Proteins

Nucleic Acids

Phospholipids

ATP

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4
Q

Electrons

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5
Q

Ionizing Radiation

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6
Q

Another form of Ionizing Radiation

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7
Q

Ionizing Radation in Medicine

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8
Q

Ultraviolet Radiation

Effect of UV Radiation

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9
Q

How much is one mole?

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10
Q

What is one molar?

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11
Q

Electrons, Protons, and Atomic Weight

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12
Q

One Molar of NaCl

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13
Q

0.14 molar NaCl

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14
Q

Normal Serum Electrolyte Reference Ranges “normal ranges”

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15
Q

mmols vs. mEq

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16
Q

What unit are Albumin Levels?

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17
Q

What unit to describe calcium levels

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18
Q

What unit describes glucose levels

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19
Q

What 2 units describes ethanol levels?

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20
Q

Equation for pH

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21
Q

Describe the significance of pH=0 and pH=14

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22
Q

Describe the basicitiy and acidity of common household items.

Describe in words what pH means.

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23
Q

What are the elements that comprise the human body?

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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?

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27
Q

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

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28
Q

Variation in size of proteins

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29
Q

Examples of Different Proteins related to their tasks

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30
Q

Enzyme Hexokinase

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31
Q

Transcription Factor

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32
Q

Structural Classifications of Proteins

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33
Q

Secondary Structure

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34
Q

Interactions comprising secondary structure

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35
Q

Primary structure. Which terminus comes first?

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Amino acids

36
Q

Primary structure is comprised of which atoms?

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37
Q

How are amino acids classified/distinguished?

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38
Q

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

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39
Q

Which components join together to form proteins?

What is this process called and what drives it?

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40
Q

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

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41
Q

Role of hydrophobic amino acids

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42
Q

What is cysteine and what is its role/function?

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43
Q

Draw out Cysteine forming a Disulfide bond

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44
Q

What is the charge of Aspartate?

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45
Q

What is the charge of lysine?

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46
Q

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

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47
Q

Draw serine out and what functional group does it contain?

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48
Q

Explain the process and significance of phosphorylation.

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49
Q

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

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50
Q

What are catalysts?

What is their role regarding the transition state?

Where are they generally located?

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51
Q

What levels of protein structure do enzymes often exhibit?

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52
Q

Where does a substrate bind?

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53
Q

Describe the induced fit model and its subsequent feedback inhibition

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54
Q

Explain competitive product inhibition

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55
Q

Allosteric site and allosteric activator/inhibitor

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56
Q

Multiple levels of regulation in metabolic pathways

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57
Q

Draw a model of allosteric activation/inhibition

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58
Q

What is a co-factor?

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59
Q

What elements make up enzymes?

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60
Q

Coenzymes

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61
Q

Coenzymes in telomerase formation

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62
Q

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

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63
Q

Role of Phospholipids

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64
Q

Role of ATP

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