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Biologia > Molecular Biology > Flashcards

Molecular Biology Flashcards

1
Q

What is an example of a compound that can be produced both by human organisms and artificially?

A

Urea!
Falsified vitalism which stated that the origin and phenomena of life are due to a vital principle that can’t be created in a lab

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2
Q

Why are carbon compounds so versatile?

A

Because they can form 4 bonds

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3
Q

What are carbohydrates?

A

Carbon compounds mposed of C, H & O2 w a 2:1 ratio of H:O

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4
Q

What are lipids?

A

C compounds that r insoluble in water

Fats are solids and oils are liquids

can be saturated which means they don’t have a double bond

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5
Q

What are proteins?

A

Carbon compounds made up of 1 (+) chain of amino acids (polypeptide)
Composed of C, H, O, N and sometimes S
Have an amino group (NH2), an R group (CHR) and a carboxil group (OCOH)

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6
Q

What are nucleic acids?

A

Carbon compounds composed of chains of nucleotides

Contain C, H, O, & P

There is RNA and DNA

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7
Q

Drawings of ribose, alpha and beta glucose

A
  • ribose: C5H10O5 start with OH on top then two OH down.
  • alpha glucose: C6H12O6 start w H at top
  • beta glucose: C6H12O6 start w H at bottom
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8
Q

what is metabolism?

A

the web of all enzyme catalyzed rxns in a cell. Most are in cytoplasm but can also be extracellular.

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9
Q

What’s catabolism?

A

breaking down of complex molecules into simpler ones. includes hydrolysis of macromolecules into monomers. Produces E.

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10
Q

what’s anabolysm?

A

The synthesis of complex molecules from simpler ones. Includes formation of macromolecules from monomers by condensation rxns. Requires E.

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11
Q

What are the properties of water?

A

Cohesion: binding together of 2 water molecules
Adhesion: bonds b/w water and other molecules that are polar
Thermal properties:
- high specific heat capacity: temp remains stable
- high latent heat vaporization: high E needed to evaporate it –> good evaporative coolant
- high boiling point: liquid at many temps

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12
Q

Compare and Contrast Methane and Water

A
  • Methane (CH4) is non polar while water (H2O) is polar.

- Methane has a lower density, specific heat capacity, latent hc, B.P /M.P

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13
Q

How is NaCl, amino acids and glucose transported in the body?

A

all carried in blood plasma
NaCl: bc ionic compound; polar so highly soluble
Amino acids: + & - charges, solubility depends on R group but can be dissolved enough
Glucose: polar; soluble

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14
Q

how is oxygen, fat and cholesterol transported in the body?

A

Oxygen: non-polar but can b dissolved due to small size. as temp increases O2 solubility decreases. hemoglobin in rbc’s has binding sites for O2
Fat: non-polar large and insoluble. carried in lipo-protein complexes w a phospholipid monolayer.
Cholesterol: insoluble. thus lipo-protein complex

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15
Q

Name 3 monosacharides

A

glucose, fructose and sucrose

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16
Q

Name 3 disacharides and their composition

A
  • Maltose (2 glucose)
  • Sucrose (glucose + fructose)
  • Lactose (glucose + galactose)
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17
Q

What is a condensation reaction?

A

a chemical reaction that requires E and results in the production of water molecules when joining molecules together.

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18
Q

What is the structure/function of cellulose?

A
  • made of B-glucoses 1-4; (polysacharide)
  • each B-glucose must be flipped –>straight chain.
  • basis of cell walls
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19
Q

What is he structure/function of Starch?

A
  • made of a-glucose 1-4 (polysacharide)
  • curved
    • amylose: helix
    • amylopectin: branched–> globular shape
  • glucose storage in plants
20
Q

What is the structure/function of glycogen?

A
  • made of a-glucose 1-4 (polysacharide)
  • curved & very branched
  • used by animals (liver and some muscles) and fungi for E storage.
21
Q

What are triglycerides and how are they made?

A
  • is an ester formed by the condensation of 3 fatty acids and 1 glycerol
  • used as E stores
  • can be released by anaerobic resp. or used as heat insulation
22
Q

Distinguish b/w E storage in lipids ad Carbohydrates

A
  • Lipids are for long term storage while carbs are better for short term.
  • Lipids store E in addipose tissue while Carbs store it in the liver and some muscles
  • amt of E released in lipids is 2x that of carbs
  • same E in lipids is 1/2 the body mass as carbs
  • lipids act as schock absorbers and are 6x more efficient
  • carbs can be used in (an)aerobic resp and are easily broken down.
23
Q

how do you calculate Body mass index?

A

BMI=mass(kg)/height(m) ^2 units are kg/m^2

24
Q

what are the different structures of fatty acids?

A 
saturated: no double bonds
unsaturated:
  -mono: 1 double bond
  -poly: 1+ double bond
      -cis: H atoms on same side
      -trans: Hs on opposite sides
25
Q

What’s coronary heart disease?

A

CHD occurs when plaque builds up in the walls of coronary arteries preventing the flow of oxygen rich blood to the heart. increases risk of heart attack

26
Q

What are polypeptides?

A

Amino acids linked together in condensation rxns. These rxns make peptide bonds. (C-N)

27
Q

Properties of polypeptides? (amino acid sequence)

A
  • there are 20 diff amino acids synthesized on ribosomes. R grp gives them character
    -amino acids can be linked in any sequence
    -the sequence of a polypeptide is coded for by genes
    -3 bases of a gene are needed to code for
    an amino acid
    -amino acid sequence determines 3D shape of a protein
28
Q

What are the diff structures of proteins?

A
  • Primary: just the peptide bonds w amino grp at one end and the carboxyl in the other
  • Secondary: a-helix or B-pleated sheet; H bonding b/w functional group
  • Tertiary: could be final structure; stable; R-group/hydro(philic or phobic) interaction; ionic/ H bonds.
  • Quaternary: min of 2 peptides joined together
29
Q

What’s denaturation?

A

permanent change to the formation of a protein.

  • heat: vibrations can cause breakage of intramolecular bonds
  • pH: charges on R groups are changed.
30
Q

What are some of the proteins (and their functions) produced by living organisms?

A
  • muscle contraction: actin and myosin
  • cytoskeletons: tubulin in microtubules
  • tensile strengthening: fibrous proteins
  • blood clotting: plasma proteins turn blood to gel
  • cell adhesion: membrane proteins cause cells to stick together
  • receptors: for senses, hormones or neurotransmitters
  • packing of DNA: histones help chromosomes condense
  • immunity: antibodies
31
Q

What are some specific examples of proteins?

A
  • Rubisco: important enzyme; CO2–> carbon compounds
  • Insulin: signals cells the need to absorb glucose; B-cells in pancreas transported by blood
  • Immunoglobin: antibdies
  • Rhodopsin: pigment that allows the absorption of light; membrane protein in rod cells
  • Collagen: rope-like protein; 3 polypeptides; provides strength
  • Spider silk: extensible and v resistant
32
Q

What is a proteome?

A

all proteins produced by a cell, tissue or organism. Its unique for every individual because of the differences in amino acid sequence

33
Q

What is genome?

A

All the genes in a cell tissue or organism

34
Q

What are enzymes?

A

globular proteins that act as catalysts. Change substrate into product. Substrate binds to active site. enzymes can only catalyze 1 rxn (enzyme-substrate specificity)

35
Q

How are substrates changed into products by enzymes?

A

catalysis involves molecular motion and the collision of substrates w the active site.

  1. substrate binds to active site of enzymes
  2. while substance is bound to active site it changes into product
  3. the product separates from active site leaving it vacant
36
Q

How does temperature affect enzyme activity?

A

Increase in temp can cause increase/decrease enzyme activity there is an optimum Temp. .

  • increase in temp. increases KE so increases chance of collision
  • too much heat will denature enzyme; bonds vibrate more leading to breakage of bonds changing its structure so that substrate can’t bind. as more enzymes fails activity stops eventually
37
Q

How does pH affect enzyme activity?

A

Most enzymes have an optimum pH which differs from enzyme to enzyme.

  • if pH increases or decreases from optimum activity will decrease
  • decrease in pH by 1 unit = 10x more acidic
  • too far from optimum can denature enzyme
38
Q

How does Substrate concentration affect enzyme activity?

A
  • An increase in substrate concentration will increase the frequency of collision which will initially increase rate.
  • the rate at which activity increases levels off because all active sites are occupied.
39
Q

how are immobilized enzymes used in industry?

A

Immobilized: attaching of the enzymes to another material; attaching them to glass; trapping them in alginate gel or boiling them to agregation.

  • enzymes and products can be easily separated, stopping rxn at ideal time, prevents contamination
  • enzymes may be recycled
  • substrates can be exposed to higher enzymes conc.
40
Q

How is Lactose-free milk produced?

A
  • lactase breaks down lactose into its components
  • milk is passed through a column containing immobilized lactase
  • enzyme is obtained from yeast that grows in milk
  • yeast is cultured and lactase is extracted and purified and enclosed in alginate beats
  • sweeter, smoother, faster production of yougurt and cheese
41
Q

How do enzymes lower Ea of the chemical rxns?

A
  • substrates must pass a transition state in order to reach this state E is required. E is also released when going from transition state to product.
  • Ea breaks/weakens the bonds in substrate
  • binding to enzyme lowers Ea
  • as Ea decreases rate of rxn increases by a factor of a million
42
Q

Compare and contrast enzyme inhibitors

A

Both reduce enzyme activity by preventing substrate to bind

  • competitive: interfere w active site so that substrate can’t bind, don’t change conformation of enzyme and have similar shape to substrate
  • non-competitive: bind at a location other than the active site, change conformation of enzyme doesn’t have similar conformation to substrate.
43
Q

How can metabolic pathways be controlled by end product inhibition?

A

allosteric interactions: are the regulation of enzymes by substances binding to an allosteric site (site away from active site)
Usually the substance is an end product of the rxn, when there is not enough product enzyme works; when there is too much it shuts down
this binding is non-competitive and reversable
* feedback inhibition

44
Q

Whats an example of end-product inhibition?

A

Threodine deaminase is the 1st of 5 enzymes required to produce isoleucine from threodine.
As isoleucine builds up it binds non-competitively/reversibly to to threodine deaminase shutting down the entire pathway.
As isoleucine is used up allosteric inhibition decreases reactivating the pathway.

45
Q

Explain the structure of DNA and RNA

A
  • polymers of nucleotides
  • 3 parts: phosphate group (circle, 5’), pentosugar (pentagon, 3’) and nitrogenous base (rectangle)
  • covalent bonds link the phosphate to pentosugar H bonds b/w nitrogenous bases
  • 4 different nucleotides which differ only by the nitrogenous base
46
Q

What are the differences between DNA and RNA

A
  • DNA is double stranded while RNA is single stranded
  • DNA has A, C, G and T while RNA is A,C,G and U
  • DNA has deoxyribose while RNA has ribose

Biologia (6 decks)

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