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Biology 1 > Biological Molecules and Enzymes > Flashcards

Biological Molecules and Enzymes Flashcards

1
Q

Hydrolysis vs dehydration

A

Macromolecule broken into smaller molecules with addition of water = hydrolysis, dehydration is opposite and water is a byproduct

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2
Q

Roles of lipids

A 
Energy storage (due to long carbon chains)
Cellular organization and structure in the membrane bc they are hydrophobic
Precursor for vitamins and minerals bc they can pass through cellular membranes
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3
Q

What is a fatty acid, Saturated vs unsaturated fatty acid

A

Building block for lipid compounds CHCHCHCOO-

Unsaturated has one or more carbon carbon double bonds

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4
Q

What are phospholipids and what are they a component of

A

Lipids with a phosphate making it polar at one end and non polar at the other (amphiphathic) therefore a good structural component of membranes

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5
Q

What do triacylglycerols do and what’s the structure

A 
Store metabolic energy and provide thermal insulation and padding 
Glycerol head (CH3) and 3 fatty acid tails
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6
Q

What do steroids (a type of lipid) do, structure

A

Regulate metabolic activities ex. Vit d, hormones, cholesterol
Four ringed

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7
Q

The fatty acid eicosanoid and terpenes can serve as

A

Hormones/signalling molecules such as prostaglandins

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8
Q

How are carbs useful, 2 examples

A

Energy source

Glucose and fructose

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9
Q

Glycogen , starch, and cellulose are____ that differ in their

A

Glucose polymers with differing linkages (alpha for glycogen)

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10
Q

Difference between nucleotide, nucleoside, and nucleic acid

A

Nucleoside is pentose(5C) sugar + nitrogenous base and nucleotide is formed with addition of phosphate. Nucleotides make up nucleic acids such as DNA

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11
Q

Purines

A

Adenine and guanine

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12
Q

Pyrimidines

A

Cytosine and thymine

Uracil (RNA)

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13
Q

Types of bonds in DNA double helix

A

Phosphodiester bond between the phosphate and carbon of sugar formed via dehydration
Hydrogens bonds between nitrogenous bases (two for AT) ( 3 for CG)

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14
Q

What is a primary structure of a protein - what types of bonds

A

Sequence of amino acids

C-N-C-N

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15
Q

Secondary structure of a protein and the type of bonds

A

Beta pleated sheet of an alpha helix

Hydrogen bonds

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16
Q

Which structure of a protein does proline effect

A

Secondary therefore also tertiary

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17
Q

6 factors contributing to tertiary structure

A
  1. Covalent disulfide bonds between 2 cystine amino acids
  2. Ionic interactions between acidic and basic side chains
  3. Hydrogen bonds
  4. Van de waals forces
  5. Hydrophobic side chains pushed from water toward center of protein
  6. R group of proline
18
Q

What does denatured protein mean

Examples of denaturing agents

A

When the native conformation of the protein is disrupted
*** rarely effects the primary structure of a protein
Ph, heat

19
Q

When you see nitrogen on the mcat think

A

Protein

20
Q

What are enzymes

A

Proteins that act as catalysts (lower the energy of activation)

** forward and reverse of reaction

21
Q

What is Vmax, how can it be increased

A

Max rate of a reaction

Increase by adding more enzymes (proportional to enzyme concentration)

22
Q

What is the Michaelis constant Km

How can we change it

A

The substrate concentration at which the reaction rate = 1/2Vmax
Inversely proportional to enzyme affinity
Can’t change with enzymes - but can be altered by certain enzyme inhibition

23
Q

Some enzymes require coenzymes to function, what are some examples

A

Minerals
Coenzymes
Vitamins

24
Q

How are enzyme reactions effected by temperature, ph and substrate concentration ** think of the graphs

A

Temp increase reaction rate until at some point the enzyme denatures
Optimal ph depends on the enzyme but generally neutral - optimal pH
Rate of reaction increases with substrate until max rate has been achieved

25
Q

What is a zymogen - think plasminogen

A

Inactive form of an enzyme that is reversed when peptide bonds are cleaved

26
Q

What is negative feedback **

A

One of the products downstream in a reaction comes back and inhibits enzymatic activity of an earlier reaction

27
Q

What is competitive inhibition and the two types

A

Competes with substrate by binding to active ** can be overcome by substrate
Irreversible (if covalent bond) and reversible

28
Q

What is uncompetitive inhibition, effect on km and vmax

A

Bind to allosteric site of the enzyme substrate complex (so only once enzyme is associated with substrate)
Decrease vmax , decreases Km

29
Q

What are mixed inhibitors

A

Bind to enzyme alone or substrate complex

30
Q

Mixed inhibitors effect on km

A

Mixed that prefer to bind to complex lower Km

Those that bind to enzyme primarily before substrate would increase Km

31
Q

What are noncompetitive inhibitors and how do they effect Km

A

Have no preference between enzyme and enzyme substrate complex
Bind to allosteric site and change conformation of enzyme
Km remains the same because they dont bind to active site

32
Q

What do you think when you see something that has ase in it on the mcat

A

Think enzyme then know it has nitrogen so is prone to denaturation

33
Q

Explain the structure of a lipoprotein

Why is it like that

A

Inside contains the triglycerides and cholesterol which is then surrounded by phospholipids. This is to transport insoluble items through the blood

34
Q

Memorize the amino acids ! Everything about them

A

Ok

35
Q

Basic amino acids at ph 7 why?

A

Lysine
Arginine
Histidine
They have an NH2(amino group) in their R group that is protonated at a ph of 7

36
Q

Acidic amino acids at ph 7 why?

A

Aspartic acid
Glutamic acid
They have a second COOH(carboxylic) group that is deprotonated at ph of 7

37
Q

Amino acid charges in relation to ph (general)

A

Low ph tend to be positively charged

High ph tend to be negatively charged

38
Q

How do enzymes effect activation energy, do they change overall free energy

A

They do not lower Ea but provide an alternate pathway with a lower Ea!!!
No dont change G

39
Q

Enzyme substrate complex has 2 different models explain them

A

Lock and key theory - substrate (reactant) fits exactly into active site of the enzymes (enzyme is bigger than the substrate)
Induced fit model - active site of enzyme changes shape as substrate binds

40
Q

Structure of glycogen, starch, and cellulose

A

Glycogen - alpha link with branching
Cellulose - beta link no branch
Starch - alpha link no branching

Biology 1 (5 decks)

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