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BIOLOGY 20 IB: UNIT D1 > D1a1: Macromolecules > Flashcards

D1a1: Macromolecules Flashcards

1
Q

Chemical of life

A

Vitamins, minerals, lipids, nucleic acid,?protein, carbohydrates

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2
Q

Dehydration Synthesis Reaction (Condensation reaction)

A

Creation of larger molecules from smaller molecules (h2o released)

Monomer(OH)+Monomer(HO)=Monomer(O)Monomer

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3
Q

Hydrolysis Reaction

A

H2O breaks larger molecules (polymers) into smaller ones (monomers). Needs water

Monomer(O)Monomers=Monomer(OH) + Monomer(HO)

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4
Q

Metabolism

A

Totality of chemical reaction in cell (provides energy and enables synthesis)

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5
Q

Anabolism

A

Builds complex molecules from simple ones (DSR)

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6
Q

Catabolism

A

Breaks complex molecules into simple ones (hydrolysis)

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7
Q

Organic componds

A

Carbon containing
•carbon can form 4 covalent bonds=large capacity
•exceptions: carbonate and oxides of carbon

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8
Q

Carbohydrates

A

•Cannot make for ourselves so we obtain from plants
•largest part of our diet
•fast energy nutrient
•”ose” suffix
•Ratio-1c:2h:1o

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9
Q

Carbohydrates structure

A

Single sugar=monomer
Chains of monomers= polymers

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10
Q

Carbohydrates: Monosaccharides

A

Sugar sugar unit (3-6c)

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11
Q

Carbohydrates: Isomers

A

Same chemical formula as monosaccharides but diff arrangements of atoms (all have c6h12o6)

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12
Q

Carbohydrates: Disaccharide

A

2 monosaccharides together

Formed by DSR (glycosidic bond formed)
Broken by hydrolysis

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13
Q

Carbohydrates: polysaccharides (3 examples)

A

Many monosaccharides where energy is stored in chemical bonds

•cellulose- plant cell walls; made of B-glucose units(linear), everyother monomer is rotated 180 degrees

•glycogen- stores carbs in animals l; made of a-glucose units (branched)

•starch- amylose (1000+ glucose and unbranched polymer) or amylopectin (1000-6000 branched glucose)

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14
Q

Lipids: Funnction

A

S- storage of energy (glycogen build up (excess carbs)=fat)
H- Hormone synthesis
I- Insulation
P- protection (cushions cells)
S- structure part of cells (cell membrane)

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15
Q

Lipid: structure

A

•Non polar
•Combined in DSR to form ester bond

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16
Q

Lipids: triglycerides

A

Glycerol+3 fatty acids
•oil- liquid at room temp
•fat- solid at room temp

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17
Q

Lipids: triglycerides (saturated)

A

Saturated fatty acid- single bind between carbon atoms (strong)

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18
Q

Lipids: triglycerides (unsaturated)

A

Unsaturated- some double bonds
•Monounsaturated-1 double bond
•Polyunsaturated- 1+ double bond
•Cis isomer- h+ on same side, double bond=kink, loosely packed
•Trans Isomer- H+ on diff sides, no kink in chain, tightly packed

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19
Q

Lipids: Phospholipids

A

Phosphate+glycerol+2 fatty acids
•negatively charged phosphate replaces one fatty acid
•head(glycerol and phosphate)= polar and soluble
•Tail(fatty acid)= non polar and not soluble

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20
Q

Lipids: waxes

A

Fatty acids (long chain) joined by long chain alcohol or carbon rings (water insoluble) ex. Waterproof coating on leaves

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21
Q

Lipids: liposomes

A

•Double layered sphere of lipids
•Can fuse with cells to deliver materials to interior
•can carry drugs to cell wo harming tissues
•gene therapy

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22
Q

Lipids: Body mass index

A

Weight range (mass in kg/height in m2)

Healthy=18.5-24.9

23
Q

Proteins: function

A

Defense, movement, catalyst, signalling, structure and transport

24
Q

Proteins: Components

A

Made of amino acids (carbon, oxygen,
Hydrogen, nitrogen, sulfur)

20=9 essential, 11 nonessential
Order and # of proteins determines type of protein

25
Q

what is a polypeptide and how is it synthesized. z what is the difference between polypeptide and a protein

A

Chain of amino acids
Synthesized on ribosomes is translation
Proteins=folded shapes of polypeptides

26
Q

Proteins: primary structure

A

Unique sequence of amino acids

27
Q

Proteins: secondary structure

A

H+ binds between peptide chain (between backbone not r group$
•pulls chain into alpha helix and beta pleated sheets

28
Q

Proteins: Types of interactions( 5 bond types)

A

•Hydrophobic- amino acids orient themselves to avoid water( towards peptide center)
•Disulphide bridge- amino acid cysteine bonds w and cysteine via its r-group
•Hydrogen Bonds- polar r-group on amino acids form bonds w another polar r-group
•Hydrophilic- Amino acids face towards water
•Ionic binds- + charged r groups bond together

29
Q

Proteins: Tertiary structures

A

Additional folding bcz of interaction between “r” groups

30
Q

Proteins: Quaternary structure

A

Large globular proteins
2+ polypeptides (same or diff)
•2=dimer and 4=tetramer (hemoglobin
•proteins fold spontaneously to become stable ( facilitated by molecular chaperones=heat shock proteins which help after denaturing which disrupts 2° and 3° bonds but not polypeptide bonds

31
Q

Proteins: denaturing conditions

A

Temp- disrupts bond sthat hold proteins together
pH- alters charge of protein, solubility and shape

32
Q

Proteins: Zwitterion

A

Has +&- charged regions

33
Q

Proteins: Coagulation

A

Permanent change

34
Q

Proteins: proteome

A

All proteins produced by cell
•Individuals has unique proteomes (diff dna=diff proteins)

35
Q

Proteins:genome

A

All genes made by cells

36
Q

Protein/Lipid:cholesterol

A

Lipoprotein =protein + lipid
•high density=good
.•low density=plaque formed in arteries

Trans fat-had to break down=obesity

37
Q

Nucleic acids

A

Hereditary and composed of nucleotides

38
Q

Enzymes (5)

A

•involved in catabolism’s bf anabolism
•add thermal energy=more collisions=occurrence of reaction more likely
•are 3-d protein and catalysts
•end in “ase” named after substrate
•reaction specific (each enzyme controls one reaction

39
Q

Catalyst

A

Increase rate of reaction wo becoming part of product or being altered itself

Reduce activation energy needed for reaction to start

40
Q

Steps of enzyme action

A
  1. Substrate binds w enzyme
  2. Enzyme undergoes conformational change
  3. Substrate converted to product
  4. Product are released
41
Q

Lock and key model

A

Enzyme acts as key to lock and unlock substrate

Substrate is complementary in shape and chemical properties which explains enzyme specificity

42
Q

Induced fit model

A

Enzyme changes shape to allow substrate to fit

Active site is not ridged and changed shape to fit substrate (conformational change=catalysis)

43
Q

Partial collision theory

A

Frequency of collisions determines rate of reaction

Increase in collision probability=increase in frequency = Increase in rate of enzyme activity

44
Q

Coenzyme

A

Assists enzyme to complete reactions

Synthesized from vitamins (organic)

Not enzyme specific

45
Q

Cofactors

A

Inorganic enzyme helpers

Not enzyme specific

46
Q

Factors affecting enzyme activity: temp

A

low temp=not enough activation energy and high temp increases rate of reaction until enzyme denatures

47
Q

Factors affecting enzyme activity: pH

A

affects charge and solubility/shape of enzyme which decreases its ability to bind w substrate

48
Q

Factors affecting enzyme activity: substrate concentration

A

high # of substrate molecules=high probability of collisions until all active sites occupied (plateau)

49
Q

Factors affecting enzyme activity: end-products concentration

A

can cause feedback inhibition (excessive end products can be poisonous)
•feedback inhibition (negative feedback)- metabolic pathways (enzymes) are controlled by end products

50
Q

Factors affecting enzyme activity: competitive inhibitors

A

Competed for active sites w substrates and halts production of products (cyanide)

51
Q

Factors affecting enzyme activity: non competitive inhibitors

A

Chemical binding to regulatory site changes shape of enzyme (allosteric activity) so substrates can’t fit anymore

Can cause feedback inhibition (activity shuts off) or precursor activity (activity proceeds if it improves fit between enzyme and substrate)

52
Q

Immobilizing enzymes

A

science can fix enzyme to surfaces to improve reaction efficiency

53
Q

Urea & Falsification of Vitalism

A

Urea- Can be produced by living organisms (Produced in liver to get rid of extra amino acids (nitrogen) and artificially synthesized (ammonia +co2=ammonium carbamate=urea+H2O

BIOLOGY 20 IB: UNIT D1 (3 decks)

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