Lecture 2 Flashcards

1
Q

Molecules of life

A

Water

Macromolecules

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2
Q

What is the solvent of life

And why

A

Water

Dissolves more molecules than any other solvent

It’s a polar molecule (opposite charge on each end)

Dissolves polar and charged molecules

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3
Q

What are the macromolecules

A

Carbohydrate
Lipids
Protein
Nucleus acids

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4
Q

Polymers of sugars

A

Carbohydrates

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5
Q

What macronutrient isn’t a polymer

A

Lipid

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6
Q

Polymers of amino acids

A

Proteins

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7
Q

Polymers of nucleotides

A

Nucleus acids

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8
Q

Polymers

A

Chains composed of molecules called monomers

Polymerize and depolymerize

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9
Q

Polymerization

A

Go from a monomer to a polymer

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10
Q

Depolymerization

A

Go from polymer to monomer

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11
Q

Polymerization/ depolymerization reactions often involve loss or addition of what

A

Water

Therefor can also be described as

Dehydration synthesis(polymerization)

Hydrolysis (depolymerization)

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12
Q

Another word for polymerization

A

Dehydration synthesis

*Synthesis means making (making polymer from monomer)

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13
Q

Another word for depolymerization

A

Hydrolysis

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14
Q

Where does addition or loss of water happen in polymerization and depolymerization

A

Happens at the binds between monomers

Known as condensation polymerization

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15
Q

Enzymes

A

Catalyze the synthesis/ hydrolysis of polymers

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16
Q

What Catalyze the synthesis/ hydrolysis of polymers

A

Enzymes

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17
Q

enzymes in synthesis/ hydrolysis of polymer

A

Polymerases

Hydrolases

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18
Q

-ase suffix =?

A

Enzyme

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19
Q

What do biopolymers look like

A

They’re not simple chains

-twist and fold up
-chains arrange into varied levels of higher order structure

Examples: DNA double helix + protein folding

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20
Q

Higher order polymer structure example- proteins

A

1° structure- amino acids chain

2° structure- ex. Helix or a sheet

3° structure- folding

4° structure- assembling with other proteins into a complex

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21
Q

What determines a proteins structure

A

Properties and order of the amino acids

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22
Q

Amino acids

A

Contain nitrogen

Mildly acidic

R= sidechain

Sidechain properties define the chemistry of proteins

23
Q

Amino acids are linked by

A

Covalent bonds called peptide bonds

24
Q

Protein AKA

A

Polypeptides

25
Q

How many different amino acids

A

20

26
Q

What causes polypeptides to twist or form sheets

A

Hydrogen bonds between nearby amino acids

27
Q

Protein twist name

A

Alpha helix

28
Q

Protein sheet name

A

Beta sheets

29
Q

Tertiary protein structure

A

Chemistry between side chains causes higher-order folding

30
Q

Quaternary protein structure

A

Individual proteins interact to form complexes

Again determined by their structure and chemistry

31
Q

Why was/is protein structure hard to predict

A

A- Central dogma of molecular biology means that for any gene we know exactly what amino acids will make up the protein

B- it’s HARD to predict what it will look like

C- it took years using X-ray crystallography to identify protein shape

D- machine learning: alpha gold and other ML based computer programs

32
Q

Cell theory

A

1-All organisms are composed of one or more cells

2- cell is the basic structural and functional unit of all living organisms

3- cells arise only from the division of pre-existing cells

33
Q

When were cells first observed

A

1600s

34
Q

Robert Hooke

A

1600s

Looked at cork cells

35
Q

Anton van Leeuwenhoek

A

Made a better microscope than Hooke and saw animacules

Animacules*

36
Q

Why are cells small

A
  • Surface area must be sufficient to allow exchange of stuff between the cell and its surroundings
  • larger volumes require more surface area to achieve this
  • larger volumes need more structural support
37
Q

Trade off between cell surface area and volume

A

As volume increases, Surface area doesn’t increase proportionally

Ex. In a cube

V= a cubed

A= 6a squared

Volume is way higher the larger a gets

38
Q

What if cells need a large surface area

A

They develop convoluted/ branch surface morphologies

Ex- brain cells, leaf epidermal cells, microvilli on intestinal epithelial cells

39
Q

What if cells need a larger volume

A

They use cell walls

Example- xylem vessels from wood

40
Q

Resolution- microscope

A

Ability of a microscope to distinguish 2 objects as being no separate

41
Q

Higher magnification increases

A

Resolution

42
Q

Higher contrast gives

A

More detail but can’t increase resolution

43
Q

Microscopy types

A

Light microscopy

Electron microscopy

44
Q

Light microscopy types

A

Reflected light

Transmitted light

Fluorescence

45
Q

Electron microscopy types

A

Transmission

Scanning

46
Q

Relflected light microscopy

A
  • stereo microscope (aka dissecting microscope)
  • lighting from top
  • can see bigger size cells
47
Q

Transmitted light

A
  • stereoscopes (some can also use light from the bottom)
  • compound microscopes
48
Q

Variations on transmitted light compound

A

1- brightfield
2- darkfield
3- phase-contrast
4- DIC (differential interference contrast aka. Nomarksi)

2-4 are:

  • contrast enhancing methods
  • exploit refractive (light scattering) properties of specimens
  • variations in specimen thickness and density influence how light passes through it
49
Q

Brightfield

A

Ones we use in the lab

Staining of term required to see more details

50
Q

Contrast enhancing methods

A

Darkfield

Phase contrast

Differential interference contrast (DIC/ nomarski)

51
Q

Dark field

A
  • illuminates sample at an angle so light does not hit the objective lens directly
  • only light that is scattered upwards by the sample reaches the objective lens
52
Q

Phase contrast

A

This method creates slight phase shifts in the illuminating light, which manifest as higher detailed images

53
Q

DIC

A

Differential interference contrast

  • similar to phase contrast
  • gives a pseudo 3D appearance