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BIOL I > CHAPTER 3 > Flashcards

CHAPTER 3 Flashcards

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1
Q

What are the molecules that make up organism?

A

proteins, carbohydrates, lipids, and nucleic acids

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2
Q

polymers

A

macromolecules

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3
Q

monomers

A

smaller molecules that create polymers

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4
Q

macromolecules

A

polymers containing thousands or more atoms

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5
Q

functional groups

A

group that has specific properties for macromolecules

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6
Q

hydroxyl

A

R-O-H; polar; hydrogen bonds with water to help dissolve molecules; enables linkages to other molecules by condensation

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7
Q

aldehyde

A

O=C-H; polar; C=O group is very reactive; important in building molecules and energy-releasing reactions

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8
Q

keto

A

O=C; polar; C=O group is important in carbohydrates and energy reactions

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9
Q

carboxyl

A

O=C-OH; charged; acidic; ionizes in living tissues to form COO- and H+; enters into condensation reactions by giving up OH-; important in energy-releasing reactions

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10
Q

amino

A

H-N-H; charged; basic; accepts H+ in living tissues to form NH3+; enters into condensation reactions by giving up H+

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11
Q

phosphate

A

O=P-O3; charged; acidic; enters into condensation reactions by giving up OH-; when bonded to another phosphate, hydrolysis releases much energy

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12
Q

sulfhydryl

A

by giving up H+, two SH groups can react to form a disulfide bridge, thus stabilizing protein structure

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13
Q

methyl

A

C-H3; nonpolar; important in interacting with other nonpolar molecules and in energy transfer

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14
Q

isomers

A

molecules with the same chemical formula, but the atoms are arranged differently
(STRUCTURAL - differ in how atoms are joined
CIS-TRANS - different orientation around a double bond
OPTICAL - mirror images)

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15
Q

condensation reactions

A

energy is used to make covalent bonds between monomers to make a polymer; a water molecule is removed

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16
Q

hydrolysis reactions

A

polymers are broken down into monomers; energy is released and water is consumed

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17
Q

polypeptide chains

A

single, unbranched chains of amino acids folded into specific 3-D shapes as defined by the sequence of amino acids

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18
Q

enzymes

A

catalyze (speed up) biochemical reactions

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19
Q

structural proteins

A

provide physical stability and movement

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20
Q

defensive proteins

A

recognize and respond to nonself substances (e.g., antibodies)

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21
Q

signaling proteins

A

control physiological processes (e.g., hormones)

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22
Q

receptor proteins

A

receive and respond to chemical signals

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23
Q

membrane transporters

A

regulate passage of substances across cellular membranes

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24
Q

storage proteins

A

store amino acids for later use

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25
transport proteins
bind and carry substances within the organism
26
gene regulatory proteins
determine the rate of expression of genes
27
motor proteins
cause movement of structures in the cell
28
amino acids
carboxyl and amino groups; function as both acid and base
29
side chains (R-groups)
have functional groups and determine where amino acids are grouped; determine how the protein can twist and fold; determine secondary and tertiary structure
30
oligopeptides (peptides)
short polymers of 20 or fewer amino acids
31
polypeptides
longer polymers
32
peptide linkages (peptide bonds)
condensation reaction that covalently bonds amino acids together
33
primary structure
sequence of amino acids
34
secondary structure
ALPHA helix - right-handed coil resulting from hydrogen bonding between N-H groups and C=O groups BETA pleated sheet - two or more polypeptide chains are aligned; hydrogen bonds form between the chains
35
tertiary structure
folding results in the specific 3-D shape; determined by interactions between R-groups; outer surfaces present functional groups that can interact with other molecules
36
denatured protein
protein that has been heated and has its secondary and tertiary structure broken down; when cooled it can return to normal because of the primary structure information and instructions
37
quaternary structure
results from interaction of subunits by all reactions
38
How do proteins bind with specific molecules?
SHAPE - there must be a general "fit" between the protein and the other molecule CHEMISTRY - surface R-groups interact with other molecules via ionic, hydrophobic, or hydrogen bonds
39
What conditions affect secondary and tertiary structure?
HIGH temperature pH CHANGES HIGH concentrations of POLAR molecules NONPOLAR substances, via HYDROPHOBIC interactions
40
How can protein shape change?
INTERACTIONS WITH OTHER MOLECULES - enzyme changes shape when it comes into contact with reactant COVALENT MODIFICATION - addition of a chemical group, such as a phosphate, to an amino acid
41
chaperones
proteins that prevent other proteins from binding to the wrong molecules after denaturation or when they are newly made and still unfolded; heat shock proteins surround a denatured protein and allow it to refold
42
carbohydrates (C1H2O1)n
-sources of stored energy -used to transport energy -carbon skeleton for many other molecules -form extracellular structures such as cell walls
43
saccharides
mono - simple sugars di - two simple sugars linked by covalent bonds oligo - 3 to 20 monosaccharides poly - hundreds or thousand of monosaccharides
44
glucose
energy source; exists as a straight chain or ring form (alpha OH down or beta OH up and can interconvert)
45
pentoses
five-carbon sugars (ribose and deoxyribose for RNA and DNA)
46
hexoses
six-carbon sugars; some are structural isomers
47
glycosidic bonds
condensation reactions that bind monosaccharides together to form disaccharides and so on
48
polysaccharides
large polymers of monosaccharides connected by glycosidic bonds; some are branches (STARCH - storage of glucose in plants GLYCOGEN - storage of glucose in animals CELLULOSE - very stable, good for structural components)
49
How can carbohydrates be modified?
addition of functional groups to form -Sugar phosphates -Amino sugars -Chitin
50
lipids
nonpolar hydrocarbons; insoluble in water; if close together, weak but additive van der Waals forces hold them together in aggregates
51
What are types of lipids?
-FATS and OILS which store energy - PHOSPHOLIPIDS which have a structural role in cell membranes -CAROTENOIDS and CHLOROPHYLLS which capture light energy in plants -STEROIDS and MODIFIED FATTY ACIDS which are hormones and vitamins -ANIMAL FAT which give thermal insulation -LIPID COATING which is around nerves and provides electrical insulation -OIL and WAX which is on skin, fur, and feathers, repels water, and slows evaporation
52
triglycerides
three fatty acids + glycerol (e.g., fats and oils)
53
fatty acid
nonpolar hydrocarbon chain with a polar carboxyl group
54
ester linkages
condensation reactions which bond carboxyls with hydroxyls of glycerol
55
saturated fatty acid
no double bonds between carbons; saturated with H atoms (animal fats; solid at room temperature)
56
unsaturated fatty acid
one or more double bonds in the carbon chain results in kinks that prevent packing (plant oils; liquid at room temperature)
57
cis fats
H atoms are on the same side
58
trans fats
H atoms are on opposite sides of the C=C bond; result from hydrogenation of vegetable oils to produce a saturated fat (e.g. for margarine), but some of the cis bonds convert to trans; may contribute to heart disease and stroke
59
omega-3 fatty acids
protect against heart disease and stroke; first C=C bond is at position 3 in the fatty acid chain
60
phospholipids
fatty acids bound to glycerol; a phosphate group replaces one fatty acid; they are amphipathic
61
amphipathic
"HEAD" - phosphate group which is hydrophilic "TAILS" - fatty acid chains which are hydrophobic
62
bilayer
in water, phospholipids line up with the hydrophobic tails together and the phosphate head facing outward (in biological membranes there is a phospholipid bilayer structure)
63
phospholipids + proteins =
lipoproteins (which transport lipids such as cholesterol in the blood)
64
carotenoids
light-absorbing pigments (e.g., beta carotene traps light energy for photosynthesis; in humans, beta carotene breaks down into Vitamin A)
65
steroids
multiple rings share carbons; cholesterol is important in membranes; others are hormones
66
waxes
long-chain alcohol bound to an unsaturated fatty acid

BIOL I (12 decks)

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