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AP Biology > Ch. 2: Chemistry > Flashcards

Ch. 2: Chemistry Flashcards

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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
Water has strong adhesion
water attracts to unlike substances as its poles attract to poles of other substances (wetting finger to turn pages) demonstrates capillary action (plants)
26
Capillary action
water's adhesion to the walls of narrow tubing or absorbent solids like paper it rises up, defying gravity
27
Organic molecules/ macromolecules
have carbon, easy to bond w/ bc 4 electrons available to form covalent bonds straight lines or rings monomers made from polymers
28
Hydroxyl group
-OH Ex.: alcohols (ethanol), glycerol, sugars polar, hydrophilic
29
Carboxyl group
-C--O/-OH Ex.: acetic acid, amino acids, fatty acids, sugars polar, hydrophilic, weak acid
30
Amino group
-N-H/-H Ex.: amino acids polar, hydrophilic, weak base
31
Phosphate group
-P--O/-O(-)/-O(-) Ex.: DNA, ATP, phospholipids polar, hydrophilic, acid
32
Methyl group
-C-H/-H/-H Ex.: fatty acids, oils, waxes nonpolar, hydrophobic
33
Monosaccharide
simplest kind of carbohydrate w/ one sugar molecule | glucose, fructose
34
Sugar molecule formula
(CH2O)N
35
Disaccharide
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
Glycosidic linkage
joins carb molecules formed by dehydration reaction that causes water molecule to be lost broken by hydrolysis reaction that requires water when
37
Polysaccharide
series of connected monosaccharides --> polymer | Ex.: starch, glycogen, cellulose, chitin
38
Starch
polymer of alpha glucose molecules | principle energy storage molecule in plant cells
39
Glycogen
polymer of alpha glucose molecules differs from starch by its pattern of polymer branching major energy storage molecule in animals
40
Cellulose
polymer of beta glucose molecules | structural molecule in walls of plant cells and wood
41
Chitin
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
Alpha-glucose vs. beta-glucose
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
Lipid solubility
insoluble in water but highly soluble in nonpolar substances
44
3 major groups of lipids
Triglycerides (triaglycerols), phospholipids, steroids
45
Triglycerides (triaglycerols)
fats and oils | 3 fatty acids (hydrocarbon chain w/ -COOH) attached to a glycerol (C2HO)
46
Fatty acid
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
Saturated fatty acid
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
Unsaturated fatty acid
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
Monounsaturated fatty acid
one double covalent bond
50
Polyunsaturated fatty acid
2+ double covalent bonds
51
Phospholipid
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
Steriod
4 carbon ring backbone | Ex. cholesterol (component of cell membranes), hormones like testosterone and estrogen
53
Types of proteins
structural, storage, transport, defensive, enzymes
54
Structural protein
Ex. keratin in hair and horns, collagen in connective tissue, silk in spider web
55
Storage protein
Ex. casein in milk, ovalbumin in egg white, zein in corn
56
Transport protein
found in membranes of cells that transport materials into and out of cells and as oxygen-carrying hemoglobin in red blood cells
57
Defensive protein
antibodies that provide protection against foreign substances in animals
58
Enzymes
regulate rate of chemical reactions
59
Protein structure (bonds)
chain of covalently bonded amino acids | bonds called peptide bonds to form polypeptide by dehydration synthesis (one H20 released in forming every bond)
60
Amino acid general form
Amino group (-NH2), Carbon w/ H, Carboxyl group (-CdoublebondOOH), R group which determines properties
61
Primary protein structure
order of amino acids
62
Secondary protein structure
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
Tertiary protein structure
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
Disulfide bonds
sulfur atom in amino acid cysteine bonds to sulfur atom in another cysteine helps maintain folds of amino acid chain
65
Quaternary structure
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
DNA
polymer of nucleotides nitrogenous base, deoxyribose sugar, phosphate group 4 DNA nucleotides each w/ its own nitrogenous base (A, T, C, G)
67
Purines
double ringed nitrogenous bases | Adenine and Cytosine
68
Pyrimidines
single ringed nitrogenous bases | Thymine and Guanine
69
Difference between RNA and DNA
1. sugar in RNA is ribose 2. uracil replaces thymine (U-A) 3. single stranded
70
Activation energy
energy needed for chemical reaction to take place (trigger formation of new bonds)
71
Catalyst
speeds up chemical reaction by lowering activation energy | does not participate in reaction so is not altered and can be re-used
72
Metabolism
chemical reactions that occur in biological systems Catabolic (break-down) and Anabolic (formations) driven by chemical equilibrium
73
Substrate
substance upon which enzyme acts | Ex. enzyme amylase catalyzes breakdown of substrate amylose (starch)
74
Enzymes
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
Induced-fit model
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
Cofactors
nonprotein molecules that assist enzymes Coenzymes: organic cofactors that accept/ donate e-, vitamins Inorganic cofactors: metal ions like Fe2+ and Mg2+
77
ATP
source of activation energy for metabolic reactions when ATP releases energy, hydrolysis reaction breaks off a P to form ADP reverse is phosphorylation
78
Reaction regulation
enzymes, feedback inhibition, competitive inhibition, noncompetitive inhibition, cooperativity
79
Allosteric effector/ Noncompetitive inhibition
binds to allosteric site on protein (NOT ACTIVE SITE) to cause conformational change in enzyme activator vs. inhibitor sometimes permanent sometimes reversible
80
Feedback inhibition
end product of a series of rxns acts as allosteric inhibitor, shutting down one of the enzymes catalyzing the rxns
81
Competitive inhibition
substance that mimics substrate inhibits enzyme by binding to active site so preventing substrate binding
82
Cooperativity
enzyme becomes more receptive to additional substrate molecules after one substrate attaches to

AP Biology (15 decks)

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