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Baron's AP Biology Terms > Chapter 2: Biochemistry > Flashcards

Chapter 2: Biochemistry Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

subatomic particles

A

protons, neutrons, and electrons

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2
Q

ground state

A

electrons are in the lowest available energy levels

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3
Q

excited state

A

electrons are in higher energy levels

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4
Q

isotopes

A

vary in number of neutrons

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5
Q

half-life

A

amount of time for half of an isoptope to decay

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6
Q

tracer

A

used to trace the path of specified molecule in metabolic pathway

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7
Q

hydrophobic

A

water hating

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8
Q

hydrophillic

A

water loving

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9
Q

properties of water

A

highly polar, hydrogen bonding, high specific heat, high heat of vaporization, universal solvent, strong cohesion, capillary action, surface tension

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10
Q

transpirational-pull cohesion tension

A

as one molecule of water is lost from a leaf by transpiration, another molecule is drawn up from roots

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11
Q

ice being less dense than water leads to…

A
  1. ice freezes: insulation of bodies of water
  2. ice melts: sinks to bottome of lake, bringing oxygen to depths and nutrients released by bacteria during winter to the surfce
    a. spring overturn: cycling of nutrients through a lake
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12
Q

buffer

A

regulates the pH of biological systems by resisting change to pH

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13
Q

isomers

A

same molecular fromula but different structure

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14
Q

structural isomers

A

differ in the arrangement of atoms

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15
Q

cis-trans isomers

A

differ in arrangement around double bonds

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16
Q

entaniomers

A

molecules that are mirror images of each other
important in the pharmaceutical industry
left-handed: L-version
right-handed: D-version

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17
Q

carbohydrates

A 
fuel for body and building materials
C,H,O
hydrogen to oxygen ratio-- 2:1
monomer: monosaccharide 
polymer: polysaccharide, disaccharide
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18
Q

dehydration synthesis

A

joining of molecules by releasing a molecule of water

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19
Q

hydrolysis

A

breakdown of compound by adding water

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20
Q

structural polysaccharides

A

plants: cellulose
animals: chitin

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21
Q

storage polysaccharides

A

plants: starch
animals: glycogen

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22
Q

lipids

A
  • hydrophobic compound that consists of 1 glycerol (alcohol) and 3 fatty acids (hydrocarbon chain with a carboxyl group at the end)
  • includes fats, oils, waxes, and steroids
  • C,H,O,N
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23
Q

saturated lipid

A
  • maximum number of H
  • no double bonds between C
  • solid at room temperature (butter)
24
Q

unsaturated lipid

A
  • doesn’t have maximum number of H
  • double bonds between C
  • liquid at room temperature (olive oil)
25
Q

steroids

A
  • lipids consisting of four fused rings

- cholesterol, testosterone, estradiol

26
Q

function of lipids

A
  • energy storage
  • structural: phospholipids (glycerol, 2 fatty acids, 1 phosphate group), cholesterol in plasma membrane
  • endocrine: some steroids are hormones
27
Q

phospholipids

A

hydrophobic tail, hydrophilic head, forms plasma membrane

28
Q

proteins

A
  • growth and repair
  • signaling from one cell to another
  • regulation through hormones
  • enzymatic activity
  • movement (actin and myosin protein fibers in muscle contractions)
  • C,H,O,N,P,S
  • monomer: amino acid
  • polymer: polypeptide (amino acids joined by peptide bonds), dipeptide
  • carboxyl, amine , R group
29
Q

protein conformation

A

shape of protein

30
Q

primary stucture

A

linear sequence of amino acids

31
Q

secondary structure

A
  • polypeptide coils or folds into alpha helix or beta pleated sheet due to hydrogen bonding within molecule
  • proteins with secondary structure are fibrous proteins
32
Q

tertiary structure

A
  • intricate 3-D shape that determines the molecules specificity
  • caused by hydrogen bonding, van der waals forces, disulfide bonds between amino acids, ionic bonding hydrophobic interactions
33
Q

quaternary structure

A
  • proteins with more than one polypeptide chain

- hemoglobin

34
Q

denaturation

A

a protein’s loss of shape due to high pH, high temperature, and high concentration of salt

35
Q

chaperonins (chaperone proteins)

A

assist in the folding of other proteins

36
Q

prions

A
  • misfolded proteins

- can cause Mad Cow Disease, Alzheimer’s, and Parkinson’s

37
Q

X-ray crystallography

A
  • scientific method of determining the precise positions/arrangements of atoms in a crystal where beams of X-ray strikes a crystal and causes the beam of light to diffract
  • technique for structure determination of proteins and biological macromolecules
38
Q

bioinformatics

A
  • uses computers and math to integrate data from amino acid sequence
  • technique for structure determination of proteins and biological macromolecules
39
Q

nucleic acids

A

-polymer for DNA and RNA (encode hereditary info)

40
Q

nucleotide

A
  • RNA and DNA monomer
  • phosphate, 5-carbon sugar (deoxyribose or ribose), nitrogenous base (adenine, thymine, guanine, cytosine, uracil)
  • C,H,O,N,P
41
Q

exergonic

A

energy is released

42
Q

endergonic

A

energy is absorbed

43
Q

metabolism

A

sum of chemical reactions that take place in cells

44
Q

catabolism

A

break down molecules

45
Q

anabolism

A

build up molecules

46
Q

pathways

A
  • series of metabolic reactions with a specific function

- controlled by enzymes, allowing for efficiency

47
Q

enzymes

A
  • catalytic proteins that speed up reactions by lowering activation energy required
  • don’t provide energy for a reaction or cause a reaction
48
Q

transition state

A

reactive (unstable) condition of substrate after sufficient energy has been absorbed to initiate the reaction

49
Q

characteristics of enzymes

A
  • globular (spherical) proteins with tertiary structure
  • substrate-specific
  • induced-fit model: wen substrate enters the active site, it causes the enzyme to change its shape to fit substrate better
  • enzyme binds to substrate, causing enzyme-substrate complex
  • enzymes are not destroyed, but reused
  • enzyme name: substrate followed by “–ase”
  • catalyze reactions in both directions
  • assisted by cofactors (inorganic) or coenzymes (vitamins)
50
Q

control of enzymatic activity

A
  • switch on/off genes that code for enzymes

- noncompetitive and competitive inhibition

51
Q

competitive inhibition

A
  • competitive inhibitors mimic substrate molecules and compete for the active site, therefore reducing productivity of enzyme
  • overcome by increasing the concentration of substrate
  • can be reversible or non-reversible
52
Q

noncompetitive inhibition

A

noncompetitive inhibitors, or allosteric regulators, bind to an alternate site distinct from the active site of an enzyme, inhibiting enzyme from catalyzing substrate into product

53
Q

allosteric

A
  • change in shape alters efficiency

- allosteric enzymes switch between active shape and inactive shape

54
Q

feedback inhibition

A

end product of the pathway is the allosteric inhibitor for an enzyme that catalyzed an earlier step in the pathway

55
Q

cooperativity

A
  • type of allosteric activation
  • binding of one substrate molecule to the active site of one subunit of the enzyme causes a change in the whole molecule that locks all subunits into active position

Baron's AP Biology Terms (14 decks)

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