Biochem Flashcards
(125 cards)
1
Q
What are living organisms made of? (organic and inorganic molecules)
A
Organic (lipids, proteins, carbs, nucleic acids, vitamins)
Inorganic (water, minerals ex. calcium, phosphorus, iron, sodium, sulfur)
2
Q
What do all organic compounds contain?
A
Carbon and hydrogen
3
Q
Where are organic compounds found?
A
In living organisms.
4
Q
What are some exceptions to the organic (CH) rule?
A
hydrocarbonates, carbonates, oxides of carbon
5
Q
What is vitalism?
A
Living organisms are different from entities cuz they contain some non-physical element (a spark or energy)
6
Q
What experiment falsified vitalism? Explain it.
A
The synthesis of urea from inorganic compounds falsified the idea that only organic compounds can make such compounds.
7
Q
What two processes make up metabolism?
A
Anabolism and catabolism
8
Q
Are ALL metabolic reactions enzyme catalyzed?
A
yes
9
Q
What is anabolism? What process does it use?
A
Anabolism is the building up of compounds (from monomers to polymers) using condensation.
10
Q
What is catabolism? What process does it use?
A
Catabolism is the breaking down of compounds (cellulose to glucose) using hydrolysis.
11
Q
What is another name for condensation?
A
Dehydration synthesis since you remove a molecule of water.
12
Q
What do hydrolysis reactions need as a reactant?
A
Water
13
Q
What do ocean waters and air currents transfer?
A
Heat
14
Q
What explains the properties of water?
A
H-bonds and dipolarity
14
Q
What are some properties of water? (3)
A
Adhesion and cohesive properties, universal solvent, thermal properties (high heat capacity, boiling and melting point)
15
Q
What two things is cohesion in water responsible for?
A
Transpiration pull, surface tension
16
Q
What is adhesion in water responsible for?
A
Transpiration pull
17
Q
What property in water makes it the universal solvent?
A
Its bent shape/polarity.
18
Q
How is glucose transported in blood? Is it polar or not?
A
Polar and dissolved in blood plasma
19
Q
How is cholesterol carried in blood? Is it polar or non-polar?
A
lipoprotein complex and is insoluble with a small hydrophilic spot.
20
Q
How are amino acids carried in the blood? Polar or non-polar?
A
Polar and dissolved in plasma.
21
Q
How are fats carried in the blood? Polar or non-polar?
A
Non-polar and inside lipoprotein complexes.
22
Q
How is oxygen transported in the blood? Polar or non-polar?
A
Hemoglobin, some dissolved in the blood. Oxygen is non-polar but small size makes it partly soluble.
23
Q
How is sodium chloride transported in the blood?
A
Dissolves in plasma.
24
What property of water allows for high boiling point?
H-bonds
25
What does it mean that water has a high specific heat capacity?
This means water can absorb/lose a large amount of energy without significantly changing the temperature of the water.
26
What are the benefits of water having a high heat capacity?
Helps organisms maintain constant temperature and regulates environmental temperature. (especially for aquatic organisms)
27
What does it mean for water to have a high heat of vaporization?
the amount of energy needed to change water from liquid to a gas is high.
28
What is having a high heat of vaporization or water good for?
Evaporative cooling, ex sweating.
29
What do the differences between water and methane arise from?
The lack of H-bonding in methane.
30
Do water and methane conduct electricity?
No, pure water should not.
31
Name 4 ways animals can get water.
Drinking, eating, cell resp, absorbing thru the skin
32
How do plants get water?
Roots
33
How do animals lose water? (4)
Breathing, sweating, feces, urine
34
How do plants lose water?
Transpiration
35
What do organisms use nutrients for?
To survive/grow
36
What are 4 macronutrients?
Carbs, lipids, proteins, nucleic acid.
37
What do macronutrients provide?
They provide the main energy and building blocks source for living organisms.
38
What are two micronutrients? What do they provide?
Water and minerals. They provide the necessary cofactors for metabolism (control body processes).
39
What are essential nutrients?
Can't be synthesized by the body and must be included in the diet.
40
What are four essential nutrients?
Dietary minerals like iron, vitamins like vitamin C in humans due to the "GULO" gene mutation, essential fatty acids, and essential amino acids.
41
What can cause rickets?
A lack of vitamin D and calcium.
42
What are two essential fatty acids? Why are they necessary?
Alpha-linolenic acid (an omega-3) and linoleic acid (omega-6). Necessary for good health.
43
How many animo acids can't be synthesized in the body?
9/20
44
What does a lack of amino acids affect?
The production of proteins.
45
What type of carbs are the macromolecules?
Starches
46
What are the building blocks of carbs?
Simple sugars and polysaccharides.
47
What are the building blocks for lipids?
Glycerol and fatty acids.
48
What are the building blocks of Nucleic Acids (DNA/RNA)?
Nucleotides
49
What are the building blocks of proteins?
Amino acids
50
What are carbs produced by?
Plants
51
What are carbs used for? (3)
Storage, energy, structure
52
What three atoms fo all carbs have?
C,H,O
53
What are 3 monosaccharides? Are they isomers?
Glucose, fructose, galactose. Yes,they are isomers.
54
What are 3 disaccharides? What monosaccharides make them up?
Sucrose (glucose and fructose), Maltose (two glucose), Lactose (glucose and galactose)
55
What are some polysaccharides? (3)
Cellulose, starch (amylose and amylopectin), glycogen (animals only)
56
Draw alpha and beta glucose.
--
57
Draw amylopectin, amylose, glycogen, cellulose.
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58
When making disaccharides from monomers, is it dehydration synthesis or hydrolysis?
Hydrolysis
59
What is the formula of a trisaccharide?
C18H32O16
60
What is the name of the bond between two sugar monomers?
Glycosidic bond
61
What is glucose used for?
ATP
62
What is lactose used for?
Sugar in milk (energy to newborns)
63
What is glycogen used for?
Energy storage in liver
64
What is fructose for?
Makes fruits sweet so animals would eat them and that leads to seed dispersal.
65
What is sucrose for?
Energy source
66
What is cellulose used for?
Component of cell walls.
67
What is the test for reducing sugars? What does a positive test look like?
Benedict's test, the more red/orange the colour, the more positive it is. The more blue/green the more negative.
68
What is the test for starch? What does a positive test look like?
Iodine (black means starch is present)
69
What are some reducing sugars?
All monosaccharides and some disaccharides like maltose and lactose.
70
What food has more than twice the energy "density" (per gram) of carbs? Why?
Lipids due to the number of chemical bonds that allow for efficient energy storage.
71
Draw all the monosaccharides.
----
72
What are some functions of lipids? (6)
Energy storage, insulation, compartment of cell membranes, protect organs, carriers of fat-soluble vitamin absorption (A, D, E, K), and steroid hormone synthesis (ex. testosterone.)
73
What is a type of lipid? What are its building blocks?
Triglyceride (one glycerol and 3 fatty acids)
74
Draw a lipid triglyceride.
----
75
What makes an unsaturated fatty acid?
The presence of a fatty acid.
76
What type of lipids are polyunsaturated fatty acids?
Oils, usually liquid, reactive, are usually thought as healthier
77
What kind of lipids are saturated fatty acids?
Animal fats, hard to break down, solid
78
What are trans fats made from?
Partially hydrogenating vegetable oils
79
Is the hydrogen on the same side or not for trans fats?
On opposite sides
80
Why are trans fats bad? (3)
Increase inflammation, LDL cholesterol and decrease HDL cholesterol
81
What are some ways to measure the presence of lipids?
Lipid test, fatometer, BMI
82
What are five examples of proteins in living organisms?
Enzymes, antibodies, pigments, hormones, structure
83
What are protein pigments for?
Rhodopsin in vision
84
What are antibodies?
immunoglobulins
85
What are some protein structures in living organisms?
Spider silk, collagen in skin
86
What makes up 50% of dry weight of organisms?
Proteins
87
How and where are proteins synthesized?
As polypeptides on ribosomes
88
What is the name of a species entire collection of proteins?
Proteome
89
What is the study of the structure, function and interaction of cellular proteins called?
proteomics
90
Sketch an amino acid.
Amine group, carboxylic group and side chain group.
91
What is the bond between amino acids called?
Peptide bond
92
What does the primary structure of a protein consist of?
Amino acid sequence (includes size of polypeptide and type of amino acids)
93
What are secondary proteins an interaction between? What type of bond is responsible for the different shapes? What are the shapes?
Between different functional groups and the H-bonds make the different shapes (alpha helix and beta sheet)
94
What are tertiary protein structures interactions between? How does this change the shape of the protein?
Interactions of the R groups (hydrogen, ionic, covalent). Provides additional folding.
95
What are quaternary structure proteins an interaction between? What is the end product?
Interactions of polypeptides, more than one tertiary polypeptide makes the protein.
96
What test is used to detect protein? What does it test for? What does a positive test look like?
Biuret test which tests for peptide bonds and will change from a blue to a purple colour if proteins are present.
97
What is the cause of PKU?
Don't have the enzyme to turn phenylalanine into tyrosine. (both types of amino acids) So, phenylalanine builds up to toxic levels causing brain damage.
98
What is starvation a result of?
A severe or total lack of nutrients/energy for the maintenance of life.
99
What is malnutrition?
used by too little (or too much) of a particular nutrient
100
What is kwashiorkar? What is it characterized by?
A form of severe protein/energy malnutrition characterized by a swollen belly.
101
What is marasmus? What is it characterized by?
A form of severe malnutrition (energy deficiency) and can be characterized by an emaciated look.
102
What is the denaturation of proteins? What can cause it? Is it reversible?
Denaturation is the change of the 3D protein shape or function due to changes in conditions like (pH or temperature). It is not reversible.
103
What can too hot of conditions due to proteins?
Too much energy can cause H-bonds and even stronger bonds to break which will change the shape of the protein.
103
How does pH affect proteins?
Too acidic or basic conditions will cause proteins to change shape.
104
Why isn't body temperature higher?
It would denature proteins.
105
Why do chemical reactions in the body need to be sped up?
Body temperature is too cold for reactions to occur efficiently.
106
What are the special catalysts in the body called?
enzymes
107
What shape are enzymes?
Tertiary and quaternary proteins
108
How do enzymes increase rate of reaction?
Lower activation energy
109
What are substrates? Active site?
enzymes have an active site to which specific substrates bind (substrates are the reactants)
110
What is the induced-fit model of enzyme action?
The active site is suited for a particular substrate.
111
What happens when the substrate binds to the active site?
A slight conformational change in the enzyme occurs.
112
What does the slight conformational change in an enzyme allow for?
Allows the catalytic parts of the enzyme to contact the necessary parts of teh substrates.
113
How does temperature affect enzyme function?
Can denature the enzyme by breaking bonds.
114
What happens when enzymes are exposed to low temperatures?
Cause enzymes to lose flexibility (lower motion/reaction rate)
115
What two factors affect reaction rate?
Substrate concentration and enzyme concentration (equal substrates and active sites for optimal function)
116
What is enzyme saturation?
When adding more enzymes does not affect reaction rate.
117
name one example of immobilized enzymes being used in industry.
lactose-free milk is made when lactase enzyme (from yeast) is immobilized and beads and regular milk is run through it
118
What are competitive inhibitors? Name an example.
Block enzyme active sites, Rubisco is inhibited by oxygen in chloroplasts.
119
What are non-competitive inhibitors?
Attach to enzyme at a site other than the active site and cause a conformational change to the active site.
120
In which type of inhibition, competitive or non-competitive, does increasing substrate concentration affect rate of reaction?
In competitive enzyme inhibition
121
What is an example of an enzyme cycle?
Photosynthesis Calvin Benson Cycle
122
How are metabolic pathways controlled?
End product inhibition. The product binds to an allosteric site.
123
What is a site on the enzyme that is not the active site called?
Allosteric site
