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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
what is a polypeptide and how is it synthesized. z what is the difference between polypeptide and a protein
Chain of amino acids Synthesized on ribosomes is translation Proteins=folded shapes of polypeptides
26
Proteins: primary structure
Unique sequence of amino acids
27
Proteins: secondary structure
H+ binds between peptide chain (between backbone not r group$ •pulls chain into alpha helix and beta pleated sheets
28
Proteins: Types of interactions( 5 bond types)
•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
Proteins: Tertiary structures
Additional folding bcz of interaction between “r” groups
30
Proteins: Quaternary structure
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
Proteins: denaturing conditions
Temp- disrupts bond sthat hold proteins together pH- alters charge of protein, solubility and shape
32
Proteins: Zwitterion
Has +&- charged regions
33
Proteins: Coagulation
Permanent change
34
Proteins: proteome
All proteins produced by cell •Individuals has unique proteomes (diff dna=diff proteins)
35
Proteins:genome
All genes made by cells
36
Protein/Lipid:cholesterol
Lipoprotein =protein + lipid •high density=good .•low density=plaque formed in arteries Trans fat-had to break down=obesity
37
Nucleic acids
Hereditary and composed of nucleotides
38
Enzymes (5)
•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
Catalyst
Increase rate of reaction wo becoming part of product or being altered itself Reduce activation energy needed for reaction to start
40
Steps of enzyme action
1. Substrate binds w enzyme 2. Enzyme undergoes conformational change 3. Substrate converted to product 4. Product are released
41
Lock and key model
Enzyme acts as key to lock and unlock substrate Substrate is complementary in shape and chemical properties which explains enzyme specificity
42
Induced fit model
Enzyme changes shape to allow substrate to fit Active site is not ridged and changed shape to fit substrate (conformational change=catalysis)
43
Partial collision theory
Frequency of collisions determines rate of reaction Increase in collision probability=increase in frequency = Increase in rate of enzyme activity
44
Coenzyme
Assists enzyme to complete reactions Synthesized from vitamins (organic) Not enzyme specific
45
Cofactors
Inorganic enzyme helpers Not enzyme specific
46
Factors affecting enzyme activity: temp
low temp=not enough activation energy and high temp increases rate of reaction until enzyme denatures
47
Factors affecting enzyme activity: pH
affects charge and solubility/shape of enzyme which decreases its ability to bind w substrate
48
Factors affecting enzyme activity: substrate concentration
high # of substrate molecules=high probability of collisions until all active sites occupied (plateau)
49
Factors affecting enzyme activity: end-products concentration
can cause feedback inhibition (excessive end products can be poisonous) •feedback inhibition (negative feedback)- metabolic pathways (enzymes) are controlled by end products
50
Factors affecting enzyme activity: competitive inhibitors
Competed for active sites w substrates and halts production of products (cyanide)
51
Factors affecting enzyme activity: non competitive inhibitors
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
Immobilizing enzymes
science can fix enzyme to surfaces to improve reaction efficiency
53
Urea & Falsification of Vitalism
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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