UNIT TEST: category 2 Flashcards

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1
Q

Function of carbohydrates in cell/body

A
  • Supply energy to cells
  • Used in plant wall cells
  • Make up human cell membrane
  • Primary source or energy
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2
Q

Function of protiens in cell/body

A
  • Catalyze chemical reactions
  • Create cell shape and organization
  • Provide energy
  • Help body repair cells
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3
Q

Function of lipids in cell/body

A
  • Part of cell membrane
  • Help move, store energy, absorb vitamines, make hormones
  • Protect organs
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4
Q

Function of nucleic acid in cell/body

A
  • Contains genetic information
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5
Q

Monomer, polymer, function groups, type of bonding, polarity of carbohydrates

A

Monomer: Glucose
Polymer: Glycogen, starch, cellulose
Function groups: Carbonyl and hydroxyl
Type of bonding: Glycosidic bonds
Polarity: polar (negitively charged end, hydrophillic)

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6
Q

Monomer, polymer, function groups, type of bonding, polarity of lipids

A

Monomer: Glycerol and fatty acids
Polymer: Trigylcerides, phospholipids, waxes, steriods
Function groups: Hydroxyl and carboxyl
Type of bonding: Ester bonds
Polarity: polar (amino acids have +/- charged ends)

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7
Q

Monomer, polymer, function groups, type of bonding, polarity of nucleic acids

A

Monomer: Nucleotide
Polymer: Nucleic acid
Function groups: Phosphate
Type of bonding: Phosphodiester bonds
Polarity: polar (neigitvly charged due to O)

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8
Q

What are ester bonds?

A
  • Bond that forms between oxygen and carbon atoms
  • Joins acids and alcohols together
  • Creates a water byproduct
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9
Q

What are ether bonds?

A
  • Oxygen molecule bonded to two alkyl or aryl groups
  • Found in carbohydrates
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10
Q

Monomer, polymer, function groups, type of bonding, polarity of protiens

A

Monomer: amino acid
Polymer: Polypeptides
Function groups: Amino and carboxyl
Type of bonding: Peptide bonds
Polarity: polar (amino has + end, carboxyl has - end)

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11
Q

What are gycosidic bonds?

A
  • Formation between H- group and -OH group
  • Releases water and links sugar units together
  • Forms polysaccharide
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12
Q

What are peptide bonds?

A
  • Bond created when carboxyl group of one molec and amino group of another molec react
  • Releases water
  • Found in protines
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13
Q

What are phosphodiester bonds?

A
  • Link between 3’ C atom of one sugar molec and 5’ C atom of another
  • Joins two sugar molecules to form polynucleotides
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14
Q

Catalytic cycle

A
  1. Enzyme available with energy active site
  2. Substrate binds to enzyme with induced fit
  3. Substrate is converted to products
  4. Products are released
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15
Q

Factors affecting enzyme activity

A

1) Temperature: Heat - assistive kinesthetic energy can denature the enzyme
2)pH: Alters ionization of peptides
3)Enzyme and substrate concentration: Saturation Level - max rate at which enzymes can combine with substrate

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16
Q

How do enzymes and substrates interact?

A

Introduced fit model: Enzymes arent rigid and active site changes before binding substrate

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17
Q

What are cofactors and coenzymes

A

Cofactors: organic molecs that help enzymes
Coenzymes: ions that help enzymes

18
Q

What are enzyme inhibiters vs activators?

A

Inhibiters: molecs that decrease activity of enzyme
Activators: molecs that increase activity of enzyme

19
Q

Types of enzyme inhibiters?

A

Competetive inhibition - molecule competes for an ezyme active site and slows down its action
Non competetive inhibtion:
1) Allosteric regulation - non competive inhibter binds to allosteric site and changes shape of active site so it no longer accepts substrates
2) Feedback inhibiton - product of biochem reaction, acts as allosteric inhiber for pathway that produced it

20
Q

Types of enzyme activators?

A

Allosteric regulation - activators bind to alosteric site and increase enzyme activity

21
Q

What are REDOX reactions?

A
  • Reaction involving the transfer of electrons
22
Q

What are hydrolisis reaction

A
  • Reaction using water
    Ex. A - B + H20
23
Q

What are hydrolisis reactions?

A
  • Reaction using water
24
Q

What are condensation reactions?

A
  • Reaction that produces water
25
Q

What is a neutrilization reaction

A
  • An acid + base converting to a salt + water
26
Q

What is the structure of cell membrane?

A
  • Phospholidis on outside and inside with polar head facing out and non-polar tailes facing in
  • Phospholipid bilayer making up cell membrane
  • Intergral membrane protiens, periphreptheral membrane protiens, protien chanels, cholestorl, glucoprotien. lipids and cytoskeletal filaments inside cell
27
Q

Cell membrane - what are protien channels used for

A

For protien to travel in and out of the cell

28
Q

Cell membrane - what is the differences between intergral and perifpreferal protiens?

A

Integral is inside of the cell, perifpreferal is outside of the cell.

29
Q

Cell membrane - What is the difference between glycoprotiens and glycolipids

A

Glycoprotiens are attatched to perifpreferal protiens, glycolipids are attatched to phospholipids

30
Q

What is the difference between active vs passive transport?

A
  • Active transport uses ATP and goes [low] to [high], secondary
  • Passive transport doesn’t use ATP and goes [high] to [low], primary
31
Q

What are the two types of passive transport?

A
  1. Diffusion (movement of solutes)
  2. Osmosis (movement of water)
32
Q

What is facilitated diffusion?

A

Molecule using energy transfers through the protien channel, out of the cell, and returns brining in another molecule. 2nd molecule does not use energy to enter the cell but the first molecule uses energy to get the second molec.
- Think groceries example

33
Q

What determines the fluidity of membranes?

A
  • Unsaturated fatty acid tails increase fluidity: unsaturated hydrocarbon tails with kinks
  • Saturated fatty acids decrease fluidity: saturated hydrocarbon tails
34
Q

What is endocytosis vs exocytisis?

A

Endocytosis: process of capturing a substance or particle from outside the cell by engulphing it in the cell membrane and brining in into the cell
Exocytosis: process of vesicles fusing with the plasma membrane and releasing their conents outside the cell

35
Q

What is osmosis?

A

Where water molecules pass through semipermeable membrane

36
Q

What are the three tonic states of osmosis?

A
  1. Hypertonic - higher solute concentration compared to intracellular salute concentration
  2. Hypotonic - lower solute concentration compared to intracellular salute concentration
  3. Isotonic - same solute concentration compared to intracellular calute concentration
37
Q

Name and draw the five functional groups

A

Check notes

38
Q

Why do we care about the functional groups inside macromolecules?

A

Functional groups are responsible for generating bonds between monomers and create polymers.

39
Q

What functional groups are in carbohydrates, and how does this effect the polarity?

A

Functional Groups: Hydroxyl and Carbonyl
Polarity: Polar and negitvly charged due to OH groups

40
Q

What functional groups are in protiens, and how does this effect the polarity?

A

Functional groups: amino and carboxyl
Polarity: Polar as amino as a (+) charged end and carboxyl has a (-) chaged end

41
Q

What functional groups are in lipids, and how does this effect the polarity?

A

Functional groups: Hydroxyl and carboxyl
Polarity: non polar as electrons are equally shared by hydroxyl and carboxyl

42
Q

What functional groups are in nucliec acids, and how does this effect the polarity?

A

Functional groups: phosphate
Polarity: Polar molecules due to negitivly charged end on phosphate