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AP Biology > Unit 2 - BioChem > Flashcards

Unit 2 - BioChem Flashcards

(81 cards)

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1
Q

covalent bond

A

sharing of valence electrons

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2
Q

molecule

A

2+ atoms held together by a covalent bond

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3
Q

compounds

A

covalent bonds between 2+ different elements

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4
Q

electronegativity

A

the attraction of an atom for the for the electrons of a covalent bond

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5
Q

non polar covalent bond

A

the electrons are shared evenly

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6
Q

ionic bond

A

the attraction for the electron is so unequal between the elements that the atom is stripped away
-formed between a cation and an anion

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7
Q
  • cations

- anions

A
  • positive charged ion

- negatively charged ion

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8
Q

hydrogen bond

A

weak bond formed by a hydrogen already in a polar covalent bond with another highly electronegative atom
O in H2O is more electronegative and therefore has a partial charge

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9
Q

van der Waals forces

A

non polar molecule

randomly all the electrons move to one side and give it momentary charges on opposite sides

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10
Q

substrate

A

reacant

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11
Q

most important elements in life

A 
Carbon
Hydrogen
Oxygen
Nitrogen
Phosphorus
Sulfur
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12
Q

trace elements

A

elements required by an organism but only in minute quantities

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13
Q

atomic number

A

of protons or electrons

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14
Q

atomic mass

A

of protons + # of neutrons

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15
Q

isotopes

A

same element with different # of neutrons

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16
Q

acid

A

substance that increases the H ion concentration in a solution

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17
Q

base

A

reduces H ion concentration
OH- bonds with a H+ and therefore reduces H+ concentration
alkaline - 14 on pH scale

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18
Q

buffers

A

resist changes in pH

weak acid and its corresponding base

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19
Q

cohesion

A

water held together by H bonds
important in transport of water against gravity
ex. water evaporates out a leaf and pulls water from the roots up

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20
Q

adhesion

A

clinging of water to a different substance

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21
Q

specific heat

A

the amount of heat needed for 1g of the substance to rise 1ºC

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22
Q

evaporization

A

transformation from liquid to gas

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23
Q

evaporative cooling

A

the surface of a molecule is left cold because the warm water evaporates (why sweating makes you cool)

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24
Q

solvent

A

dissolving agent

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25
solute
substance being disolved in
26
hydrogen shell
each dissolved ion is surrounded by a sphere of water molecules
27
functional groups
attachments that replace 1 or more hydrogen atoms in the carbon skeleton
28
go read functional groups flashcards
RN
29
aldelhyde
carbonyl group is at end of carbon skeleton
30
ketone
carbonyl group is in the middle of the skeleton
31
why are carbon atoms so versatile?
make 4 covalent bonds
32
hydrocarbons
molecules only consisting of carbons and hydrogens
33
isomers
molecules with same molecular formula but different structures
34
structural isomers
same molecular formula but different covalent arrangement of atoms
35
geometris isomers
same covalent arrangement but different spacial arrangment
36
cis | trans
both geometric isomers same side of C chain opposite side
37
enantiomers
molecules that are mirror images of eachother
38
carbohydrates
simple sugars and polymers
39
what do nucleotides consist of?
nitrogen base, pentose sugar, 3 phosphate groups
40
monosaccharides - components - ending - classified by... - use
simple sugars - carboxyl group & hydroxyl groups - ose - # of carbons in backbone - fuel
41
4 major macromolecules
carbohydrates, lipids, proteins, & nucleic acids
42
bond that links monomers to become polymers
covalent
43
condensation / dehydration synthesis reaction | -enzyme used
uses energy to attach new monomer to chain by taking away hydroxyl group from 1 monomer and H from the other to make H2O -polymerase
44
hydrolysis | -enzyme used
breaks bonds holding monomers together (H2O required) | -hydralase
45
use in transporting monomers through cell membrane
enzyme through hydrolysis breaks into monomers which can enter the cell inside the cell dehydration reactions create polymers
46
alpha v. beta hydroxyl groups
alpha is a downwards bond | beta is upwards (difficult to hydrolyse)
47
sucrase lactase maltase
enzymes that speed up the hydrolysis of | sucrose, lactose and maltose
48
chitin
used in exoskeletons of arthopods
49
lipids
hydrophobic (non polar covalent bonds)
50
saturated fatty acid
no double C-C bonds (H @ every possible position)
51
unsaturated
double C=C bond that causes a kink
52
fat | -use
LIPID - oils are unsaturated and liquid fat is solid and saturated because takes more heat (nrg) to break them down -stores energy, cushions vital organs
53
phospholipids - hydrophobic - hydrophilic
2 fatty acids attacked to a glycerol and a phosphate group at the 3rd position - head (phosphate has - charge) - tail
54
phospholipid bilayer
head on outside and tails on inside | -barrier between cell and external environment
55
proteins
made from 20 different monomers (amino acids) | polypeptide
56
amino acid | -peptide bond
4 components attached to a central C * R group (specific to the amino acid) * H atom * carboxyl group - CHO2 * amino group NH2 - dehydration reaction removes hydroxyl group and hydrogen
57
x-ray crystallography
used to determine protein conformation
58
anti parallel strands
the 2 DNA strands are parallel but go in different directions
59
polysaccharides | -function
energy storage and building material for the cell | -hydrolyze and break off sugar as needed
60
starch | -glycogen
storage polysaccharide composed of only glucose monomers (alpha) -animal starch
61
cellulose
polysaccharide with alternating alpha beta, making it strong and hard to break
62
fatty acid | -triglyceride
carboxyl group attached to long carbon skeleton | - 3 fatty acids joined to a glycerol
63
proteins levels of structure - primary - secondary - tertiary - quaternary
- sequence of amino acids - shapes of single strands (coils and folds) - shape changes based on interactions between R groups - 2+ strands making shapes
64
purines v. pyrimidines | -who bonds with who
Purines - 2 rings: A&G Pyrimidines - 1 ring: C & t & U -A with T -G with C
65
carbohydrates | -produced how
source of energy. polymers and simple sugars | -photosynthesis
66
metabolism
the total of an organisms chemical reactions
67
catabolic pathways
release energy by breaking down molecules
68
anabolic pathways
use energy to make complex molecules
69
thermodynamics
the study of energy transformations
70
entropy
measures disorder and randomness
71
exergonic rxn
net release of free enegry
72
endergonic rxn
absorbs free enegry
73
catalyst
changes the rate of a reaction without being consumed in the rxn
74
cofactors
non protein helpers required by enzymes
75
coenzymes
organic cofactors | ex. vitamins
76
inhibitors
prevent enzymes from catalyzing rxns
77
competitive inhibition
inhibitor binds to active site so substrate can't
78
noncompetitive inhibition
inhibitor binds somewhere other than active site causing it to change shape and become inactive
79
allosteric site
not active site | molecules binding here change the shape of the enzyme - either make it work or not
80
activators
stabilize the conformation
81
feedback inhibition
pathway is turned on or off by presence of product or substrate

AP Biology (4 decks)

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