Ch. 2: Chemistry Flashcards

1
Q

Atom

A

nucleus of positively charged protons and neutrally charged neutrons with negatively charged electrons outside nucleus

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2
Q

Molecules

A

groups of two or more atoms held together by chemical bonds,

formed by interaction of their electrons

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3
Q

Electronegativity

A

ability of an atom to attract electrons,

plays large part in determining kind of bond formed

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4
Q

Ionic Bond

A

electrons transferred,

electronegativities v different and one atom has much stronger pull on electron (high electronegativity)

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5
Q

Ion

A

atom with charge;

gain electron –> (-) lose electron –> (+)

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6
Q

Covalent Bond

A

electrons between atoms shared,

electronegativities between atoms are similar

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7
Q

Nonpolar Covalent

A

electrons shared equally,

electronegativities are equal and atoms pull equally, (O2)

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8
Q

Polar Covalent

A

electrons shared unequally, atoms have different electronegativities so one pulls electron more

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9
Q

Pole

A

during polar covalent bond, atom with greater electronegativity holds electrons closer and produces a negative charge (pole); other atom forms positive pole
Example: H20 (O more electronegative)

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10
Q

Hydrogen Bond

A
weak bonds between molecules
form when (+) charged H atom in one covalent molecule is attracted to a (-) area of another covalent molecule
in water (+) H forms H bond w/ (-) O of another molecule
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11
Q

Properties of water

A
excellent solvent
high specific heat capacity
ice floats
has strong cohesion and high surface tension
has strong adhesion
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12
Q

Water as solvent

A

ionic substances soluble in water bc poles of water molecules separate them into ions, polar covalent molecules work similarly
so many molecules dissolve in water –> universal solvent

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13
Q

Hydrophilic

A

“water loving,” dissolve in water because are charged

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14
Q

Hydrophobic

A

“water fearing,” nonpolar covalent substances lack charged poles and do not dissolve in water

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15
Q

Solute

A

substance that dissolves solvent

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16
Q

Aqueous solution

A

water is the solvent

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17
Q

Specific heat

A

degree to which a substance changes temperature in response to gain or loss of heat

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18
Q

Water’s high specific heat

A
changes temperature v slowly w/ changes in heat content
have to add large amounts of energy to warm water or remove lots to cool
evaporative cooling (sweat)
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19
Q

Water changing state

A
when heated (solid-->liquid-->gas) energy is absorbed and breaks H bonds, keeping temp. constant
when cooled this is reversed, and H bonds are formed with the released energy
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20
Q

Heat of fusion

A

energy requited to change water from solid to liquid

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21
Q

Heat of vaporization

A

energy required to change water from liquid to gas

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22
Q

Ice floats

A

water expands as it freezes and becomes less dense than the liquid form
weak H bonds constantly break and reform in liquid state while in ice, H bonds between water molecules become rigid in a honeycomb arrangement

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23
Q

Implications of ice floating

A

if ice didn’t float it would sink and remain frozen due to the insulating protection of the overlaying water so would profoundly affect the survival of the organisms living at the bottom of the water

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24
Q

Water has strong cohesion and surface tension

A

H bonds cause cohesion and water sticks together, this forms high surface tension so creating a water surface firm enough to allow many insects to walk upon w/out sinking

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25
Q

Water has strong adhesion

A

water attracts to unlike substances as its poles attract to poles of other substances (wetting finger to turn pages)
demonstrates capillary action (plants)

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26
Q

Capillary action

A

water’s adhesion to the walls of narrow tubing or absorbent solids like paper it rises up, defying gravity

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27
Q

Organic molecules/ macromolecules

A

have carbon, easy to bond w/ bc 4 electrons available to form covalent bonds
straight lines or rings
monomers made from polymers

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28
Q

Hydroxyl group

A

-OH
Ex.: alcohols (ethanol), glycerol, sugars
polar, hydrophilic

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29
Q

Carboxyl group

A

-C–O/-OH
Ex.: acetic acid, amino acids, fatty acids, sugars
polar, hydrophilic, weak acid

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30
Q

Amino group

A

-N-H/-H
Ex.: amino acids
polar, hydrophilic, weak base

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31
Q

Phosphate group

A

-P–O/-O(-)/-O(-)
Ex.: DNA, ATP, phospholipids
polar, hydrophilic, acid

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32
Q

Methyl group

A

-C-H/-H/-H
Ex.: fatty acids, oils, waxes
nonpolar, hydrophobic

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33
Q

Monosaccharide

A

simplest kind of carbohydrate w/ one sugar molecule

glucose, fructose

34
Q

Sugar molecule formula

A

(CH2O)N

35
Q

Disaccharide

A

carbohydrate w/ 2 sugar molecules linked by glycosidic linkage
glucose + fructose = sucrose (table sugar)
glucose + galactose = lactose (milk)
glucose + glucose = maltose (breakdown of starch)

36
Q

Glycosidic linkage

A

joins carb molecules
formed by dehydration reaction that causes water molecule to be lost
broken by hydrolysis reaction that requires water when

37
Q

Polysaccharide

A

series of connected monosaccharides –> polymer

Ex.: starch, glycogen, cellulose, chitin

38
Q

Starch

A

polymer of alpha glucose molecules

principle energy storage molecule in plant cells

39
Q

Glycogen

A

polymer of alpha glucose molecules
differs from starch by its pattern of polymer branching
major energy storage molecule in animals

40
Q

Cellulose

A

polymer of beta glucose molecules

structural molecule in walls of plant cells and wood

41
Q

Chitin

A

polymer similar to cellulose but each beta glucose has nitrogen-containing group attached to ring
structural molecule in walls of fungus cells and in exoskeleton of insects, arthropods and mollusks

42
Q

Alpha-glucose vs. beta-glucose

A

alpha glucose: starch (alpha-glycosidic linkages all OH on same side) can easily be broken down (digested) by humans and animals –> helical structure
beta glucose: cellulose (beta-glycosidic linkages every other OH flipped) can only be broken down in specialized organisms –> unbranched sheets that form H bonds

43
Q

Lipid solubility

A

insoluble in water but highly soluble in nonpolar substances

44
Q

3 major groups of lipids

A

Triglycerides (triaglycerols), phospholipids, steroids

45
Q

Triglycerides (triaglycerols)

A

fats and oils

3 fatty acids (hydrocarbon chain w/ -COOH) attached to a glycerol (C2HO)

46
Q

Fatty acid

A

hydrocarbons with a carboxyl group (-COOH) at one end of the chain
vary in structure by # of carbons and placement of single and double covalent bonds between carbons

47
Q

Saturated fatty acid

A

have only single bonds between carbons so saturated w/ hydrogen
as a result can pack together more tightly –> higher melting temps and solid at room temp (fats)

48
Q

Unsaturated fatty acid

A

have double bonds between carbons which creates a bend at bond, spreading triglyceride apart
so have lower melting temp and liquid at room temp

49
Q

Monounsaturated fatty acid

A

one double covalent bond

50
Q

Polyunsaturated fatty acid

A

2+ double covalent bonds

51
Q

Phospholipid

A

triglyceride but w/ phosphate group (-PO3^2-) in place of one of fatty acid chains
fatty-acid “tails” are nonpolar & hydrophobic
phosphate “head” is polar and hydrophilic
oriented so that tails on inside and heads on outside, making cell membranes

52
Q

Steriod

A

4 carbon ring backbone

Ex. cholesterol (component of cell membranes), hormones like testosterone and estrogen

53
Q

Types of proteins

A

structural, storage, transport, defensive, enzymes

54
Q

Structural protein

A

Ex. keratin in hair and horns, collagen in connective tissue, silk in spider web

55
Q

Storage protein

A

Ex. casein in milk, ovalbumin in egg white, zein in corn

56
Q

Transport protein

A

found in membranes of cells that transport materials into and out of cells and as oxygen-carrying hemoglobin in red blood cells

57
Q

Defensive protein

A

antibodies that provide protection against foreign substances in animals

58
Q

Enzymes

A

regulate rate of chemical reactions

59
Q

Protein structure (bonds)

A

chain of covalently bonded amino acids

bonds called peptide bonds to form polypeptide by dehydration synthesis (one H20 released in forming every bond)

60
Q

Amino acid general form

A

Amino group (-NH2), Carbon w/ H, Carboxyl group (-CdoublebondOOH), R group which determines properties

61
Q

Primary protein structure

A

order of amino acids

62
Q

Secondary protein structure

A

3D shape of protein from H bonding between amino and carboxyl groups of nearby amino acids
Spiral alpha helix bc H on one side only of Beta pleated sheets bc alternating H so H bonds form

63
Q

Tertiary protein structure

A

additional 3D shaping
often dominates shape of globular proteins
caused by: H bonding/ ionic bonding between R groups in amino acids, hydrophobic effect that occurs when hydrophobic R moves toward center of protein, disulfide bridges

64
Q

Disulfide bonds

A

sulfur atom in amino acid cysteine bonds to sulfur atom in another cysteine
helps maintain folds of amino acid chain

65
Q

Quaternary structure

A

protein made from 2+ separate peptide chains

Ex. hemoglobin that’s made of 4 peptide chains held by H bonds and interactions among R groups

66
Q

DNA

A

polymer of nucleotides
nitrogenous base, deoxyribose sugar, phosphate group
4 DNA nucleotides each w/ its own nitrogenous base (A, T, C, G)

67
Q

Purines

A

double ringed nitrogenous bases

Adenine and Cytosine

68
Q

Pyrimidines

A

single ringed nitrogenous bases

Thymine and Guanine

69
Q

Difference between RNA and DNA

A
  1. sugar in RNA is ribose
  2. uracil replaces thymine (U-A)
  3. single stranded
70
Q

Activation energy

A

energy needed for chemical reaction to take place (trigger formation of new bonds)

71
Q

Catalyst

A

speeds up chemical reaction by lowering activation energy

does not participate in reaction so is not altered and can be re-used

72
Q

Metabolism

A

chemical reactions that occur in biological systems
Catabolic (break-down) and Anabolic (formations)
driven by chemical equilibrium

73
Q

Substrate

A

substance upon which enzyme acts

Ex. enzyme amylase catalyzes breakdown of substrate amylose (starch)

74
Q

Enzymes

A

substrate specific (lock-and-key), unchanged in reaction, can catalyze rxn in both forward and backward direction, efficiency affected by temp. and pH (denaturation)

75
Q

Induced-fit model

A

describes how enzymes work
enzyme has active site with which reactants (substrates) readily interact, substrate causes conformational change of enzyme that places substrate in a more favorable position to react

76
Q

Cofactors

A

nonprotein molecules that assist enzymes
Coenzymes: organic cofactors that accept/ donate e-, vitamins
Inorganic cofactors: metal ions like Fe2+ and Mg2+

77
Q

ATP

A

source of activation energy for metabolic reactions
when ATP releases energy, hydrolysis reaction breaks off a P to form ADP
reverse is phosphorylation

78
Q

Reaction regulation

A

enzymes, feedback inhibition, competitive inhibition, noncompetitive inhibition, cooperativity

79
Q

Allosteric effector/ Noncompetitive inhibition

A

binds to allosteric site on protein (NOT ACTIVE SITE) to cause conformational change in enzyme
activator vs. inhibitor
sometimes permanent sometimes reversible

80
Q

Feedback inhibition

A

end product of a series of rxns acts as allosteric inhibitor, shutting down one of the enzymes catalyzing the rxns

81
Q

Competitive inhibition

A

substance that mimics substrate inhibits enzyme by binding to active site so preventing substrate binding

82
Q

Cooperativity

A

enzyme becomes more receptive to additional substrate molecules after one substrate attaches to