Bio 110 Chapter 3 (3.8-3.16) Flashcards

1
Q

lipids are

A

water insoluble
hydrophobic
contain twice as much energy as a polysaccharide

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2
Q

lipids are important in

A

long-term energy storage

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3
Q

lipids consist mainly of

A

carbon and hydrogen atoms linked by nonpolar covalent bonds.

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4
Q

lipids differ from carbohydrates, proteins and nucleic acids because

A

they are not macromolecules, not built from similar monomers.

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5
Q

lipids vary a great deal in

A

structure and function

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6
Q

3 types of lipids

A

fats, phospholipids, and steroids.

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7
Q

a large lipid made from glycerol and 3 fatty acids

A

fat

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8
Q

glycerol is

A

an alcohol with 3 carbons that each have an -OH

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9
Q

a fatty acid is

A

a carboxyl group and a hydrocarbon chain 16 or 18 carbon atoms in length.

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10
Q

synonym for fat

A

triglyceride

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11
Q

a fatty acid can link to a glycerol by a

A

dehydration reaction

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12
Q

fatty acids containing one or more double bonds are

A

unsaturated fatty acids

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13
Q

double bonds in fatty acids cause

A

kinks or bends in the chain
prevent them from packing together tightly and solidifying at room temperature.
fewer hydrogen atoms because of the double bond.

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14
Q

fats with the max number of hydrogens are called

A

saturated fatty acids

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15
Q

unsaturated fats include

A

corn and olive oils

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16
Q

unsaturated fats include

A

most animal fats

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17
Q

hydrogenated vegetable oils are unsaturated fats that have been

A

converted to saturated fats by adding hydrogen (margarine)

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18
Q

hydrogenation creates

A

trans fats associated with health risks.

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19
Q

phospholipids are

A

structurally similar to fats and the major component of all cell membranes.

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20
Q

phospholipids are structurally similar to fats in that:

A

phospholipids contain 2 fatty acids instead of 3 attached to glycerol, but a phosphate group is attached to glycerol’s 3rd carbon.

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21
Q

hydrophilic and hydrophobic ends of multiple molecules assemble in a

A

bilayer of phospholipids to form a membrane.

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22
Q

The phospholipid bilayer is formed by

A

the hydrophobic tails of the fatty acids clustering in the center and the hydrophilic phosphate heads facing the watery environment on either side of the membrane.

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23
Q

lipids in which the carbon skeleton contains 4 fused rings

A

steroids

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24
Q

a common component in animal cell membranes and starting material for making other steroids, including sex hormones

A

cholesterol.

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25
too much cholesterol can contribute to
atherosclerosis
26
anabolic steroids
synthetic variants of testosterone can cause a buildup of muscle and bone mass often prescribed to treat anemia and diseases that destroy body muscle.
27
abuse of anabolic steroids include
mood swings, depression, liver damage, cancer, high cholesterol and HBP.
28
proteins are
involved in nearly every dynamic function in your body and are very diverse
29
a protein is
composed of differing arrangements of a common set of 20 amino acid monomers, and is a polymer of amino acids.
30
amino acids have
an amino group and a carboxyl group (which makes it an acid.)
31
bonded to the alpha carbon in an amino acid is:
an amino group a carboxyl group a hydrogen atom and R group
32
an R group is
the side chain,differs with each amino acid and determines the specific properties of each of the 20 amino acids found in proteins.
33
amino acids are classified as
hydrophobic (nonpolar) | hydrophilic (polar)
34
amino acid monomers are linked together to form
polymers by dehydration reactions.
35
the dehydration reaction in amino acids
joins the carboxyl group of one amino acid to the amino group of the next with a peptide bond.
36
peptide bond
covalent bond between amino acids
37
a chain of 3 or more amino acids is called a
polypeptide.
38
most polypeptides are at least
100 amino acids in length; some are 1000 or more.
39
functioning proteins are
1 or more polypeptide chains coiled, twisted and folded into a 3D shape.
40
A polypeptide is not the same as a
protein.
41
probably the most important role for proteins is as
enzymes
42
Enzymes serve as
metabolic catalysts, and increase the rate of a chemical reaction without undergoing any permanent chemical change itself, regulate chemical reactions within cells
43
provide associations between body parts
structural proteins
44
found within muscles
contractile proteins (movement)
45
include antibodies of the immune system
defensive proteins
46
coordinate body activities through cell communication
signal proteins (hormones and other chemical messengers)
47
transmit signals into cells, may be built into cell membranes
receptor proteins
48
proteins that carry oxygen
transport proteins (hemoglobin)
49
serve as a source of amino acids for developing embryos
storage proteins
50
determines the protein's specific function
the shape of the protein like a lock and key
51
if a protein's shape is altered, it
can no longer function.
52
the process where a polypeptide chain unravels or loses it's shape and therefore function is
denaturation
53
can cause denaturation of proteins:
change in salt concentration, pH or high heat.
54
4 levels of structure in a protein
primary secondary tertiary quaternary
55
the primary structure is
its unique sequence of amino acids
56
the unique sequence of amino acids is determined by
the cell's genetic information (genes)
57
slightest change in amino acids in a protein can result in
changes in the protein's ability to function
58
sickle cell results from
change to hemoglobin's primary structure
59
secondary structure results from
coiling or folding of the polypeptide.
60
coiling of a protein results in
an alpha helix
61
folding of a protein results in a
beta pleated sheet (in spider webs)
62
coiling and folding are maintained by
regularly spaced hydrogen bonds between H atoms and O atoms along the backbone of the polypeptide chain, giving strength.
63
beta pleated sheets make
the core of globular and fibrous proteins
64
proteins can have various combos of
alpha helix and beta pleated sheets.
65
tertiary structure is
the overall 3D shape of a polypeptide.
66
tertiary structure results from
interactions between R groups
67
disulfide bridges (covalent bonds) may further
strengthen the protein's shape.
68
quaternary structure
when 2 or more polypeptide chains (subunits) associate.
69
when proteins fold incorrectly
disease can result.
70
collagen has 3 helices giving
strength.
71
collagen makes up
40% of protein in the human body.
72
the amino acid sequence of a polypeptide is programmed by
a discrete unit of inheritance known as a gene
73
Genes consist of
DNA-a type of nucleic acid
74
DNA provides
directions for its own replication and genetics are passed on to each daughter cell.
75
DNA programs a cell's activities by
directing the synthesis of proteins.
76
DNA does not
build proteins directly
77
RNA
transcribes DNA, and is translated into proteins.
78
functions of proteins
``` structure movement storage defense transport hormones receptors enzymes ```
79
RNA is translated in the
nucleus of eukaryotic cells and the cytoplasm of prokaryotic cells
80
DNA and RNA are composed of
monomers called nucleotides
81
nucleotides have
3 parts
82
3 parts of a nucleotide
a 5 carbon sugar (ribose in RNA and deoxyribose in DNA) a phosphate group a nitrogenous base
83
DNA nitrogenous bases are
adenine thymine cytosine guanine
84
RNA has
uracil instead of thymine
85
a nucleic acid polymer is
a polynucleotide
86
a polynucleotide forms
from nucleotide monomers when the phosphate of one nucleotide bonds to the sugar of the next by dehydration reactions, resulting in a repeating sugar-phosphate backbone with protruding nitrogenous bases.
87
2 polynucleotide strands wrap around each other to
form a DNA double helix
88
Base pairs
A and T C and G
89
most people stop producing
lactase early in childhood, and can't digest the milk sugar in lactose.
90
researchers identified 3 mutations that
keep the lactase gene permanently turned on.
91
Lactase gene mutations appear to have occurred
7,000 years ago at the same time domestication of cattle appeared in regions where dairy was available year round.