Ch.3 Carbon and the Molecular Diversity of Life Flashcards
(132 cards)
1
Q
living organisms consist mainly of
A
carbon-based compounds
2
Q
organic compound
A
compound containing carbon
3
Q
macromolecules
A
carbohydrates, nucleic acids, proteins
4
Q
four main organic compounds
A
carbohydrates, lipids, proteins, nucleic acids
5
Q
shape of carbon bonded to 4 atoms
A
tetrahedral
6
Q
basis of living molecules
A
carbon, hydrogen, oxygen, nitrogen
7
Q
shape of carbon double bonded to 2 atoms
A
linear shape
8
Q
carbon forms
A
large, complex, and diverse molecules
9
Q
carbon skeleton
A
carbon chain that forms most organic molecules
10
Q
carbon linking to other carbon atoms
A
carbon chain
11
Q
hydrocarbon
A
organic molecule consisting only of carbon and hydrogen
12
Q
many organic molecules (particularly fats)
A
have hydrocarbon components
13
Q
hydrocarbons undergo reactions
A
that release large amount of energy
14
Q
isomer (enantiomer, cis-trans, structural)
A
compound that has same number of atoms of the same element but different structures and properties
15
Q
structural isomer
A
isomer that differs in covalent arrangement of atoms, isomers increase as carbon skeleton grows
16
Q
cis-trans isomer
A
carbons have covalent bonds to the same atoms but atoms have different spatial arrangement due to inflexibility of double bond (double bonds can only go in certain areas)
17
Q
cis trans isomer can affect
A
activities of organic molecules
18
Q
enantiomer
A
isomer that is mirror image of same element but differs in shape due to presence of asymmetric carbon
19
Q
only one enantiomer isomer is
A
biologically active
20
Q
left handed and right handed version of the same element
A
enantiomer
21
Q
replaces one or more hydrogens bonded to carbon skeleton of hydrocarbon
A
chemical group
22
Q
functional group
A
the chemical groups that affect molecular function by being directly involved in chemical reactions, participates in chemical reaction in characteristic way
23
Q
hydroxyl group
A
OH
24
Q
carbonyl group
A
C=O
25
carboxyl group
C=O and OH
26
amino group
NH₂
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sulfhydryl group
SH
28
phosphate group
OPO₃ ² ⁻
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methyl group
CH₃
30
adenosine triphosphate, ATP
organic molecule with important function in cell
31
ATP structure
organic molecule called adenosine attached to a string of 3 phosphate groups
32
ATP releases energy when
it reacts with water, breaking bond between one phosphate group and the other 2
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adenosine diphosphate
adenosine with 2 phosphates instead of 3 after one phosphate's bond is broken to create energy
34
macromolecules
polymers built from building blocks called monomers
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polymer
substance that has molecular structure of many similar units bonded together
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monomer (building block)
molecule bonded to other identical monomers to form a polymer, some monomers have functions of their own
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cells make and break down polymers by
dehydration and hydrolysis reactions
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dehydration reaction (opposite of hydrolysis reaction)
occurs when two monomers bond together through loss of a water molecule
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hydrolysis reaction (opposite of dehydration reaction)
occurs when polymers are disassembled to monomers through addition of a water molecule
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hydrolysis and dehydration reactions facilitated by
enzymes
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enzyme
acts as catalyst that speeds up chemical reactions
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carbohydrates include
sugars and polymers of sugars
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monosaccharide (simple sugar)
simplest carbohydrate
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carbohydrate macromolecule
polysaccharide polymer composed of many monosaccharide monomers
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most common monosaccharide
glucose
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monosaccharide molecular formula
multiples of CH₂O
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monosaccharides classified by
number of carbons in skeleton and placement of carbonyl group (C=O)
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hexose
6 carbon sugar (glucose/fructose)
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pentose
5 carbon sugar
50
in aqueous solutions, sugars form
rings
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carbohydrates drawn as
linear skeletons
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disaccharide
formed when dehydration reaction joins 2 monosaccharides
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glycosidic linkage
type of covalent bond that joins carbohydrate molecule to another group
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2 main roles of polysaccharides
storage and structure
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polysaccharide roles determined by
sugar monomers and position of glycosidic linkages (bonds)
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starch (plant)
storage polysaccharide of plants made up by glucose monomers
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surplus starch stored as
granules
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animals can use glucose from starch through
enzymes that hydrolyze plant starch making it back into glucose
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glycogen (animals)
storage polysaccharide of animals stored mainly in liver and muscle cells
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polymers of glucose
starch, glycogen, cellulose
61
cellulose (plants)
structural polysaccharide in plants, major component of tough plant cell walls
62
fats are hydrophobic because
they are made up of hydrocarbons, which are nonpolar and not attracted to polar charges of water
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unsaturated fats are liquid because
they have carbon double bonds which changes their shape
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saturated fats are solid because
they contain as much hydrogen as possible with no carbon double bonds
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ionic bond can occur in a protein's
amino acids, NH3 and O
66
complementary base pairing
nitrogenous bases of DNA pairing up to form hydrogen bonds
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starch, glycogen, and cellulose all have glucose monomers but differ because of
different glycosidic linkages and 2 ring forms of glucose
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α glucose (helical)
glucose monomers in starch and glycogen are linked in ring formation through hydroxyl group (OH) on bottom of ring
69
β glucose (straight molecules)
glucose monomers in cellulose are linked in a ring formation through hydroxyl group (OH) alternating between top and bottom of linked rings
70
cellulose hydroxyl groups (OH) on glucose monomers can hydrogen bond with hydroxyl groups of adjacent cellulose molecules forming
microfibrils
71
microfibril
strong building material for plants held together as parallel cellulose molecules
72
through hydrolyzing α linkages of starch, enzymes can
break starch into glucose monomers and use it for energy
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enzymes are not able to hydrolyze β linkages so cellulose
passes through digestive tract as insoluble fiber
74
chitin
structural polysaccharide found in exoskeleton of arthropods and provides structural support for cell walls of fungi
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lipids don't form true polymers because
the different elements of lipids are just very close together, not actually bonded
76
lipids have no affinity for
water (hydrophobic)
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most important lipids
fats, phospholipids, and steroids
78
major function of fats
energy storage as it is compact way to carry energy stores
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fats are constructed from 2 smaller molecules
glycerol and fatty acids
80
fatty acid
carboxyl group (COOH) attached to long hydrocarbon skeleton
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glycerol
3 carbon alcohol with hydroxyl group (OH) attached to each carbon
82
ester linkage
process of dehydration reaction between glycerol and fatty acid, linking them together
83
triacylglycerol/triglyceride
3 fatty acids joined to glycerol by ester linkage, each fatty acid bonds to hydroxyl group of glycerol
84
fats separate from water molecules because
water molecules hydrogen bond to each other and exclude fats
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different fatty acids vary in
number of carbons and in number and location of double bonds
86
phospholipid
two fatty acids and a phosphate group attached to a glycerol (3 hydroxl groups)
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phospholipid bilayer
two hydrophobic fatty acid tails and hydrophilic phosphate group head assemble into phospholipid bilayer with hydrophobic tails pointing towards interior
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phospholipids are very important in
cell membranes as bilayer arrangement of cell membranes acts as boundary between cell and environment
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steroid
lipid characterized by carbon skeleton consisting of 4 fused rings
90
cholesterol (important steroid)
component in animal cell membranes which can be bad in humans with too much
91
protein
biologically functional molecule that consists of one or more polypeptides coiled, twisted, and folded into unique shape
92
polypeptides can be shown through 3 models
ribbon model, space filling model, and wireframe model
93
polypeptide
unbranched polymer built from same set of 20 amino acids
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amino acid
organic molecule with carboxyl group (COOH, C terminus) and amino group (NH2, N terminus) that differs in properties due to side chains called R groups
95
amino acids are linked by
peptide bonds which string amino acids together into polypeptide
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3 levels of protein structure
primary, secondary, tertiary + extra quaternary
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primary protein structure
sequence of linked amino acids
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secondary protein structure
2 types with either α helix or β pleated sheet
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β pleated sheet
2 or more segments of polypeptide chain lined up together forming sheet like structure through hydrogen bonds
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α helix
amino acid chain arranged in a spiral because of hydrogen bonds between amino group and oxygen from carboxyl group
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tertiary protein structure
determined by interactions of side chain R groups including disulfide bridges, hydrogen bonds, ionic bonds, and hydrophobic interactions
102
quaternary structure
occurs when protein consists of 2 or more polypeptide chains and results from interactions among multiple chains
103
change in primary structure (amino acid sequence)
affects protein structure and ability ot function
104
sickle cell disease
inherited blood disorder that results from single amino acid substitution in sequence of hemoglobin protein
105
3 factors that affect protein structure
amino acid sequence, physical conditions, chemical conditions
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denaturation
loss of protein's original structure which causes it to become biologically inactive, can sometimes renature with favorable conditions
107
protein functions
defense, storage, structure, transport, cellular communication, movement
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enzymatic protein
accelerates chemical reactions (digestive enzyme)
109
defense protein
protects against disease (antibody)
110
storage protein
starch and glycogen which store glucose for energy
111
transport protein
transportation of things (hemoglobin)
112
hormonal protein
coordination of organism's activities (insulin)
113
receptor protein
cell response to chemical stimuli (nerve cell receptors)
114
contractile and motor proteins
movement (actin/myosin)
115
structural protein
support (chitin, cellulose)
116
gene
unit of inheritance that programs amino acid sequence of polypeptide, made of DNA
117
2 types of nucleic acids
RNA and DNA
118
RNA (ribonucleic acid)
copy of double helix DNA strand that travels as mRNA to make proteins
119
DNA (deoxyribonucleic acid)
provides direction for replication and directs synthesis of mRNA to control protein synthesis
120
polynucleotide
nucleic acid polymer made of monomers called nucleotides
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nucleotide
each nucleotide consists of pentose sugar (5 carbon), nitrogenous base, and one or more phosphate group
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nitrogenous base
has one or two rings that include nitrogen atoms
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2 types of nitrogenous bases
pyrimidines and purines
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purine nitrogenous bases
adenine and guanine
125
pyrimidine nitrogenous bases
cytosine, thymine, uracil
126
nucleoside
portion of nucleotide without phosphate group (pentose sugar and nitrogenous base)
127
prime '
identifies carbon atoms in ribose
128
adjacent nucleotides joined together by covalent bonds between 3' hydroxyl group of sugar and 5' of phosphate
links sugar and phosphate group with nucleotide appendages forming half of double helix
129
RNA molecules exist as
single polypeptide chains
130
DNA molecules have
2 polynucleotides forming double helix
131
antiparallel structure
base of double helix as 3' polypeptide links to 5' polypeptide
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contemporary base pairing
nitrogenous bases in DNA pair up through hydrogen bonds
