Unit 2 - Biochemistry Flashcards

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1
Q

The 4 main classes of macromolecules

A

Proteins, carbohydrates, nucleus acid, and lipids

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2
Q

Polymers

A

Made up of similar repeating subunits
^ The macromolecules

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3
Q

Monomer

A

Simplest unit that makes up a polymer
— Lego, prices form a polymer

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4
Q

Carbohydrates
- their monomer
- their 3 monosaccharides

A

Body’s primary source of energy
Their monomers are monosaccharides (single sugar)
The 3 monosaccharides are glucose, galactose, and fructose

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5
Q

Maltose
Lactose
Sucrose

A

M- glucose glucose
L- glucose galactose
S- glucose fructose

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6
Q

Polysaccharides

A

Carbohydrates containing more than 2 sugars (also called complex carbohydrates)
Starch, cellulose and glycogen

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7
Q

How to recognize carbo hydrates

A

1) Carbon carbon backbone
2) repeating ring structures
3) ending the the suffix ‘ose’

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8
Q

Animals producing carbohydrates?

A

Animal cells cannot make the they must consume them, all food particles must be converted to a single glucose monomer
Glucose is the only molecule that can be used by the cristae

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9
Q

Glycogen

A

The body stores excess blood glucose in cells as glycogen
A polysaccharide containing repeating glucose subunits
- Formed by 2 hydroxyl groups (OH) from neighbouring glucose molecules releasing water as a byproduct

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10
Q

Dehydration synthesis

A

Process of creating a polymer by losing water

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11
Q

Hydrolysis

A

Process where a molecule is broken apart by reacting with water
- uses this to break glycogen into single glucose molecules when the blood is low (on glucose)

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12
Q

What do they contain when they have the Prefix ‘glyco’

A

Mixture of CH and some other macromolecule

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13
Q

Proteins

A

Provides structure (structural proteins) and speeds up chemical reactions in the body (enzymes)

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14
Q

Monomers of proteins

A

Amino acids
- these bond together through peptide bonds (formed through dehydration synthesis)
- group of connected amino acids = polypeptide

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15
Q

Amino and acid group

A

Peptide bonds join the amino group of one amino acid to the acid group of another amino acid

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16
Q

How do amino acids differ

A

Side chain
R-group

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17
Q

How to recognize protein
And their function

A

Recognized by a C-C-H back bone
Function depends on shape

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18
Q

What happens when a proteins shape is denatured

A

It’s said that it’s shape has been changed in a way it reduces function

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19
Q

Coagulation

A

Process of irreversibly denaturing a protein (egs. Cooking)
Preteens can be denatured through either changes in temperature or pH

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20
Q

Enzymes

A

Protein responsible for preforming chemical reactions
- body needs to preform 200,000 chemical reactions to survive

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21
Q

Homestastis

A

The normal state of the body
- Blood pH 7.38
Body temp 36.7
Fasting blood sugar level 4-7 mM

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22
Q

Active state

A

Location on the enzyme where a chemical reaction occurs

23
Q

Substrate

A

Reactants of an enzymatic reaction

24
Q

Helper molecules

A

Some enzymes need helper molecules in order to catalyze reactions

25
Q

Cofactors

A

Inorganic (no carbon) helper molecules such as Iron and zinc

26
Q

Coenzymes

A

Organic (carbon based) helper molecules such as vitamins

27
Q

How is enzymatic activity increased

A

Concentration
More substrate = more product

28
Q

Feedback inhibition

A

Where enzymatic activity decreases
- to much product blocks substrate from attaching to the active site

29
Q

Competitive inhibition

A

Decrease’s enzymatic activity by filling the active site with molecules called inhibitors (which mimic the shape of a substrate)
- often used in pharmaceuticals

30
Q

Buffers

A

Chemical pairs that prevent large changes in pH
- one chemical in the buffer pair neutralizes the acids while the other neutralizes bases

31
Q

Lipids and their defining characteristics

A

Used for energy, storage, insulation and hormone synthesis
- insoluble (doesn’t dissolve) and immiscible (doesn’t mix) in water

32
Q

Polar

A

Most chemicals in body are polar especially water
- they contain a partially positive end and a partially negative end due to an i Raquel sharing of electrons

33
Q

Are lipids polar

A

No they are non-polar (do not contain unequal charges)

34
Q

What happens when polar molecules (protein) interact with water

A

The partial negatives of the proteins bind to the partial positives of the water (and vice versa)
- non-polar molecules done interact this way so no mixing or dissolving occurs

35
Q

Fats
Oils

A

F- solid lipids at room temp
O- liquid lipids at room temp

36
Q

What are the 2 monomers of lipids

A

Glycerol and fatty acids

37
Q

Triglycerides

A

Simplest lipids, containing one glycerol and 3 fatty acids joined through dehydration synthesis

38
Q

Phospholipid

A

Type of lipid in which one of the fatty acids have been replaced by a phosphate group
- phosphate = very negative, so one end of the lipid is polar (soluable in water)
- this is the primary component of cell membrane, ideal for controlling transportation of molecules in and out

39
Q

Phospholipid bilayer
- Hydrophilic heads and Hydrophobic tails

A

In cell and nuclear membranes there are 2 sheets of phospholipids = phospholipid bilayer

  • the phosphate heads are hydrophilic (likes water) since they are polar and interact with water molecules
  • the fatty acid tails are hydrophobic (fears water) since they are non-polar and don’t interact with water
40
Q

Passive transport

A

Movement across a membrane without use of energy
- diffusion and osmosis

41
Q

Diffusion

A

Moment of a substance from high to low concentration
- the molecules that are transported are not affected by the cell
- molecules that use diffusion to cross cell membrane are oxygen, carbon dioxide and urea

42
Q

Osmosis

A

Diffusion of water

43
Q

Tonicity

A

Concentration of dissolved molecules in water

44
Q

Solute

A

Dissolved ions, macromolecules, etc
- ver full of solute inside the cell usually meaning that tonicity is higher inside cell than outside

45
Q

Isotonic solutions

A

The same solute concentration as the inside of the cell and the outside
(Water goes in and out the same)

46
Q

Hypotonic solutions

A

Lower solute concentration (therefore higher water concentration) than inside of the cell
- water molecules move from the hypotonic soln into the cell, causing cell expansion and possibly bursting

47
Q

Hypertonic solutions

A

Higher solute concentration (lower water concentration) than inside the cell
- water molecules move from the cell to the hypertonic solution causing cell the shrink and shrivel

48
Q

Active transport

A

Movement of particles across a membrane with the use of energy
- required if molecules are being transported against the concentration gradient, or if molecule is to large to move across membrane on its own

49
Q

Why does active transport require carrier proteins

A

these are embedded in the cell membrane and transport molecules across once activated
- for very large molecules the cell membrane must form vacuoles for transport
(these vacuoles are formed by folding the cell membrane around the target molecules, then detaching the newly formed pocket)

50
Q

Exocytosis

A

Release of cellular materials from the cell by forming an external vacuole

51
Q

Endocytosis

A

The intake of large particles by forming a vacuole along the cell membrane

52
Q

Pinocytosis

A

The endocytosis of liquid particles (often lipids)

53
Q

Phagocytosis

A

The endocytosis of solid particles