Unit 4 Flashcards

(60 cards)

1
Q

How many cellulose do plants produce per year?

A

100 billion tons cellulose/year
= the most abundant organic compound

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2
Q

Why is cabon a good molecular building block?

A
  • it is chemically versatile (can form single, double, triple bonds)
  • carbon-carbon bonds = very strong and perfect for macromolecules.
  • carbon-carbon bonds also allow for the rotation of the molecule
  • carbon skeletons can vary immensely, which is crucial to obtaining molecular complexity/diversity.
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3
Q

Organic molecule is __________?

A

Molecules formed by the actions of living things and/or have carbon backbone.

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4
Q

What is a biomolecule’s carbon skeleton?

A

Carbon atom bonding to other carbon atoms forms the “carbon skeleton”

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5
Q

Which property of the molecule does the carbon skeleton influence?

A

the shape of the molecule

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6
Q

Describe 2 ways that carbon skeletons can differ.

A

They can vary in
- length
- branching
- double bond position
- presence of rings

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7
Q

Define a monomer and a polymer.

A

Macromolecules are chain/like molecules called polymers (for all 4 classes of life’s organic compounds, except for lipids)

polymer = long molecule with many similar blocks linked by covalent bonds.

monomer =small blocks that are linked to form the polymer.

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8
Q

What reactions build polymers (+ describe them)

A

Dehydration synthesis
= 2 molecules are bonded covalently to each other with the loss of a water molecule.

1 monomer provides the -OH group, while the other provide a -H.

This reaction is repeated as monomers are added to the chain, making a polymer.

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9
Q

What is the range in size and complexity of biomolecules? And the basis for such diversity

A

Many macromolecules, each formed from 40-50 different monomers = diversity.

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10
Q

The 4 major classes of biomolecules:

A
  • carbohydrates (fuel and building material)
  • lipids (hydrophobic)
  • proteins (molecular tools of the cell)
  • nucleic acis (informational polymers)
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11
Q

State 2 functional classes for polysaccharides in organisms & describe the use of each.

A

Energy storage
- plants: starch = a polymer of glucose monomers. (glucose=cellular fuel-> starch = stored energy)
the sugar can be withdrawn by hydrolysis (=breaks the bonds between glucose monomers)

  • animals: glycogen = polymer of glucose.
    vertebrates store glycogen it liver/muscle cells.

structural
- plants: cellulose= polysaccharide in cell walls
polymer of glucose formed by glycosidic linkages
-insects,spiders: chitin

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12
Q

What is the general structure of a monosaccharide? Give examples

A

Mono:
- single unit sugars
- (CH2O)n, where n is between 3 and 6

  • triose = 3 C = glyceraldehyde
  • pentoses = 5C = ribose
  • hexoses = 6C = glucose/galactose/fructose
  • glucose= most common monosaccharides
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13
Q

What is an isomer?

A

2 molecules wih the same number of atoms&elements but different structures&proprieties. ex: glucose vs fructose vs galactose
Fructose is more sweet

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14
Q

Polysaccharides:
- general structure
- 2 functional classes
- Describe the use of each in organisms

A

polymers with monosaccharides joined by glycosidic linkages.
- storage
-structural

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15
Q

storage or structural polysaccharides :
- starch
- glycogen
- cellulose
- chitin

A

starch = storage
glycogen = storage
cellulose= structural
chitin= structural

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16
Q

Why many animals cannot digest structural polysaccharides?

A
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17
Q

Which types of organisms can digest structural polysaccharides?

A

A cow = carries prokaryotes and protists that can digest cellulose in its gut.

these microbes hydrolyze the cellulose ingested from hay/grass and convert the glucose to other compounds that nourish the cow.

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18
Q

What mechanism do herbivores use to digest cellulose in plants.

A

Herbivores don’t produce enymes to break down cellulose.
Instead, they have procaryotes (bacteria) in their digestive system, which have enzymes to brak it down.

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19
Q

List :
- the unifying feature of lipids
- 3 classes of lipids based on structure and function

A
  • hydrophobic
  1. steroids
  2. Phospholipids
  3. neutral fats
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20
Q

Describe neutral fats (composition + functions)

A

large molecule assembled from small molecules by dehydration synthesis

1 triglyceride fat = 1 glycerol + 3 fatty acids = true hydrophobic and covalent bond

energy storage
-> Animals convert excess sugars into fats

insulation
-> Whales/seals have thick layers of fat

protection of internal organs
-> Fragile organs are protected by a layer of fat (ovaries)

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21
Q

What determines the shape of triglyceride?
(room temperature?)

A

the saturation of the carbon chains

“saturated” every carbon in the chain has a maximum amount of H bound to it.
-> no double bond
-> straight and stackable fatty acid.
-> saturated fatty acid = solid at room temperature

“unsaturated”
-> double C-C bond
-> reduces the # of H that can bond to a C atom
-> bent fatty acid

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22
Q

What is the general structure of a fat (the 2 kinds of smaller molecules).

A
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23
Q

Compare the structure of a saturated fat to an unsaturated fat. Indicate whether each type of fat is solid or liquid at room temperature

A

“saturated” every carbon in the chain has a maximum amount of H bound to it.
-> no double bond
-> straight and stackable fatty acid.
-> saturated fatty acid = solid at room temperature

“unsaturated”
-> double C-C bond
-> reduces the # of H that can bond to a C atom
-> bent fatty acid
-> liquid at room temperature

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24
Q

What are the 3 functions of fat (adipose) tissue in animals?

A
  • energy storage
    -insulation
    -protection of internal organs
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25
Describe the function of oil in plants.
26
What is the structure of Phospholipids?
2 fatty acids + 1 glycerol. composed of : - 1 phosphate group with a negative charge = hydrophilic - fatty acids = neutral charge = hydrophobic
27
What is the structure of steroids?
lipids that have a carbon skeleton consisting of 4 fused rings.
28
What are 2 functions of cholesterol in animals?
Cholesterol serves as a building block from which other steroids (sex hormones) are synthesized. Its main function is to maintain the integrity and fluidity of the cell membrane = help the body make cell membranes and hormones
29
What is a function for steroids in animals (apart from chloesterol) +give examples.
30
Why are phospholipids amphipathic?
amphipathic because: hydrophilic head that is a charged phosphate group, polar so interacts with water hydrophobic fatty acid tails that won't interact with water
31
What happens when phospholipids are added to water? Which structure do they form?
32
What is the major function of phospholipids in all organisms?
33
What are anabolic steroids?
+++ growth of skeletal muscle (anabolic effect) +++ develop male sexual characteristics (androgenic effect) side effects: - heart attack - liver cancer - rage - delusions - depression - hair loss - acne - increase breasts - decrease size genital - masculine body
34
List the 8 functional classes of proteins + description + examples. STD CRESH
Storage Transport Defensive Contractile and motor Receptor Enzymatic Structural Hormonal
35
What is the general structure of an amino acid?
2 main groups of aa's - nonpolar -> hydrophobic - polar -> hydrophilic
36
What differentiates one amino acid from another?
The R group ("side chain") differs from one aa's to the other. The R group determines the unique characteristics of an aa's
37
What is the primary structure of a polypeptide?
specific aa's sequenece of a protein sequenece = determined by our genes
38
What is the relationship between primary structure and the higher order structures of proteins?
The primary structure = determined by inherited genetic information. The chemical nature of the backbone + side chains (R groups) of the aa's along the polypeptide allows it to dictate secondary and tertiary structure.
39
What is the secondary structure of a protein? what type of bonds result in the secondary structure?
- segments of a protein's peptide chain are coiled or folded. - these coils/folds contribute to the protein's overall shape. - results from hydrogen bonds between the constituents of the polypeptide backbone (not aaà,s side chains). - 2 types of secondary structure; alpha helix beta pleated sheet
40
What is the tertiary structure of a protein. What drives the protein into its tertiary structure?
The overall 3D shape of a polypeptide. = results from interactions between the side chains (R groups) of the aa's. = The final folded shape of the protein is determined by : 1. hydrophobic interactions 2. covalent bonds ("disulfide bonds") 3. Ionic bonds 4. Hydrogen bonds hydrophobic interactions with water drive the protein into its tertiary structure.
41
What is the quaternary structure of a protein? give 2 examples of protein with a 4th structure
- the overall protein structure - only for protein with 2 or + polypeptide chains. - results from the aggregation of polypeptide subunits. examples - collagen has 3 identical helical polypeptides interwined into a larger triple helix. - hemoglobin
42
What is denaturation and its effect on protein function?
Protein structure depends on the physical/chemical conditions. Change in pH/temperature may destroy the weak chemical bonds and interactions within a protein. Denatured protein has its polypeptide chains unraveled. = results in the lost of their specific shape. = results in the lost of their function. i.e: making meringue from an egg/ cooking an egg.
43
Storage protein role + examples
Storage - Storage of amino acids - casein = protein of milk = source of aa's for baby mammals - ovalumin = protein of egg white used to develop embryo
44
Transport protein role + examples
Transport -transport of substances - hemoglobin = protein of vertebrate blood that transports oxygen.
45
Defensive protein role + examples
Defensive -protection against disease - antibodies inactivate and help destroy viruses/bacteria
46
Contractile and motor protein role + examples
Contractile and motor - movement - motor protein cause undulations of cilia and flagella - actin & myosin = contraction of muscle
47
Receptor protein role + examples
Receptor -response of cell to chemical stimuli - receptors in the membrane of a nerve cell = detect signaling molecules
48
Enzymatic protein role + examples
Enzymatic - selective acceleration of chemical reactions -digestive enzymes = catalyze the hydrolysis of bonds in food molecules
49
Structural protein role + examples
structural -support -keratin= protein of hair,horns,feathers. - silk fibers = insects and spiders cocoons/webs - collagen and elastin = protein used in animal connective tissues
50
Hormonal protein role + examples
hormonal -coordination of an organism's activities - insulin = hormone secreted by the pancreas= causes other tissues to take up glucose and regulate blood sugar concentration
51
What are the charges of the polypeptide backbone? (secondary structure)
The oxygen atoms= partial negative charge The hydrogen atoms attached to the nitrogen have a partial positive charge. Allows hydrogen bonding to occur.
52
How strong are the h-bonds in the polypeptide backbone?
Individually= weak But bc there are so many of them, they are strong enough to maintain the shape of the protein
53
Name 3 monomers -> polymers series
1. monosaccharides -> polysaccharides 2. aa's -> protein 3. nucleotides -> nucleic acid
54
1 polymer is constructed from ___ to ___common _________________
1 polymer is constructed from 40 to 50 common monomers (= A,B,C,D,E -> WORD)
55
What reaction breakdown polymers? +describe it
Hydrolysis = reverse of the dehydration synthesis a water molecule is added, which breaks the bond between monomers. a hydrogen from water gets attached to one monomer and the OH group gets attached to the other. example: process of digestion ; enzymes attack the food (polymers), and thus releases monomers that are then absorbed into the bloodstream.
56
Macromolecules are constructed by _________ _______ monomers by _________ synthesis
Macromolecules are constructed by covalently bonding monomers by dehydration synthesis
57
Which class of large biological molecules does not consist of polymers?
Lipids
58
What is the general structure of a polysaccharide? Give examples
2 monosacharrides bonded by glycosidic linkage (dehydration reaction) glycosidic linkage = covalent bond i.e: - 1 monomer glucose + 1 monomer glucose = 1 maltose disaccharide - 1 monomer glucose + 1 monomer fructose = 1 sucrose disaccharide
59
______ can digest cellulose in soil, thereby recycling chemical elements in the Earth's ecosystem.
Fungi can digest cellulose in soil, thereby recycling chemical elements in the Earth's ecosystem.
60