Chapter 2 Flashcards
(114 cards)
1
Q
Alpha particle
A
2 protons and 2 neutrons / equivalent to a Helium nucleus
2
Q
Beta particle
A
Free electron
3
Q
Physical half-life
A
The time required for 50% of its atoms to decay to a more stable state
4
Q
Biological half-life of a radioisotope
A
Time required for half of it to disappear from the body/ by radioactive decay and by excretion
5
Q
Ion
A
Charged particle with unequal number of protons and electrons
6
Q
Electrolytes
A
Substances that ionize in water (axis, bases, and salts) and form solutions capable of conducting electricity
7
Q
Free radicals
A
Chemical particles with an odd number of electrons
Ex. O_2^- / 2 Oxygens with an extra electron
8
Q
Ionizing radiation
A
Radiation that ejects electrons from atoms, converting atoms to ions / in high doses, it can be mutagenic and carcinogenic
9
Q
Antioxidant
A
Chemical that neutralizes free radicals
10
Q
Molecular weight (MW)
A
MW of a compound is the sum of the atomic weights of its atoms (amu)
11
Q
Ionic bond
A
Attraction of a cation to an anion
Ex: Na+ and Cl-
12
Q
Covalent bonds
A
Form by the sharing of electrons
Ex: H_2
13
Q
Hydrogen bonds
A
Weak attraction / slightly+ Hydrogen and slightly- Oxygen or Nitrogen
14
Q
Van dee Waals forces
A
Weak, brief attractions between neutral atoms b/c of fluctuations in electron movements / plastic wrap / works in large pieces
15
Q
Compound
A
???
16
Q
Solvency
A
The ability to dissolve other chemicals
Water is the “universal solvent”
17
Q
Hydrophilic
A
Able to dissolve in water
18
Q
Hydrophobic
A
Substances that do not dissolve in water
19
Q
Adhesion
A
The tendency of one substance to cling to another
Water adheres to the body’s tissues and forms a lubricating film
20
Q
Cohesion
A
The tendency of molecules of the same substance to cling to each other
Water creates an elastic layer on top called Surface Film held together by Surface Tension
21
Q
Chemical reactivity of water
A
It’s ability to participate in chemical reactions
Water Ionizes chemicals such as acids and salts / also ionizes itself to take part in Hydrolysis and Dehydration Synthesis
22
Q
Thermal stability
A
TS of water helps to stabilize the internal temperature of the body. It results from high Heat Capacity of water(amount of heat required to raise the Temp 1•C)
23
Q
calorie (cal)
A
1 cal is the amount of heat that raises the temperature of 1 g of water 1•C
24
Q
Solution
A
Consists of particles of matter (solute) mixed with a more abundant substance (solvent)(usually water) Particles are under 1 nm Do not scatter light much/ transparent Pass through most sel.perm.membr Does not settle Ex: glucose in blood
25
Colloid
```
1-100 nanometers in size
Scatter light so are usually cloudy
Cannot pass through semiperm.membr
Permanently mixed
Ex: albumin in plasma (proteins in H2o)
```
26
Suspension
```
Ex: blood
Suspended particles exceed 100nm
Cloudy or opaque
Too large to pass through s-p-membr.
Not permanently suspended
```
27
Emulsion
Suspension of a liquid in another
| Blood/ mothers milk
28
Molarity (M)
of moles per liter of solution
29
Milliequivalents per liter (mEq/L)
| electrolytes in our body fluids
Millimolar concentration of an electrolyte times valence of the ion
30
Acid
Proton donor, a molecule that releases an H+ in water
31
Base
Proton acceptor / or hydroxide (OH) donor
32
pH
Derived from [molarity] of H+
| pH is the negative log of hydrogen ion molarity
33
Buffers
Chemical solutions that resist changes in pH / weak acid/ weak base
34
Ion trapping / pH partitioning
An uncharged compound such as aspirin is in the acid of the stomach, it passes easily through the cell membrane to the blood; but when it hits the more basic pH of the blood, it ionizes and gets trapped in the bloodstream
35
Energy / kinetic / potential
The capacity to do work
energy of motion, energy to do work
Energy contained in an object b/c of its position or internal state but that is not doing work at the time
36
To do work
To move something, whether it is a muscle or a molecule
37
Chemical energy
Potential energy stored in the bonds of molecules
38
Heat
The kinetic energy of molecular motion/ temp is the measure of rate of this motion
39
Electromagnetic energy
Kinetic energy of moving "packets" of radiation called "photons"
Ex: light
40
Electrical energy
Kinetic and potential forms
Potential energy when in a battery
Kinetic when they begin to move or generate electrical current
41
Free energy
Potential energy available in a system to do useful work
| Ex: in human physiology, the energy stored in the chemical bonds of organic molecules
42
Chemical reaction
Process in which a covalent or ionic bond is formed or broken
Has reactants and products
Affected by: concentration, temperature, and catalysts
43
Law of Mass Action
Reversible reactions proceed from the reactants in greater quantity to the substances with the lesser quantity
44
Metabolism
All chemical reactions in the body
Catabolism
Anabolism
45
Catabolism
Consists of energy-releasing decomposition reactions
| E-releasing reactions are "exergonic"
46
Anabolism
Energy-storing synthesis reactions
Ex: production of protein and fat
"Endergonic"
47
Oxidation
Reaction in which a molecule give up electrons and releases energy
Receiver of the electron is oxidizing agent
48
Reduction reaction
Molecule gains electrons and energy
| When molecule accepts electrons it is reduced / the one that donates them is the reducing agent
49
Carbon backbones
Long chains, branched molecules, and rings
| Can form H-, O-, N-, S- covalent bonds
50
Hydroxyl group
-OH
| Sugars/alcohols
51
Methyl
-CH3
| Fats, oils, steroids, amino acids
52
Carboxyl group
-COOH
| Amino acids, sugars, proteins
53
Amino
-NH2
| Amino acids, proteins
54
Phosphate
-H2PO4
| Nucleus acids, ATP
55
Polymers
Molecules made of a repetitive series of identical or similar subunits called "Monomers"
Formation is "polymerization"
56
Dehydration synthesis (condensation)
Living cells achieving polymerization by this means
| Hydroxyl group removed from one monomer and a H from another producing water as a by-product
57
Hydrolysis
Opposite of dehydration
Water molecules ionize into OH- and H+, breaking the covalent bond
All digestion consists of these
58
Carbohydrate
Hydrophilic organic molecule with the general formula (CH2O)n where n represents the number of carbon atoms
59
Monosaccharides
| C6 H12 O6 -first three
```
Glucose - blood sugar
Fructose - fruit sugar/converted to glucose
Galactose - converted to glucose
Ribose -
Deoxyribose -
```
60
Disaccharides
Two monosaccharides/ breaks down
Sucrose (Gl+Fr) - table sugar
Lactose (Gl+Ga) - milk sugar/babies
Maltose (Gl+Gl) - starch digestion
61
Oligosaccharides
Short chains of 3+ monosacc.
62
Polysaccharides
Long chains of monosacc. (50+ish)
63
Glycogen
Energy-storage polysaccharide made by cells of the liver, muscles, brain, uterus, and vagina
Only polysaccharide found in human tissue
64
Starch
Energy-storage polysaccharide of plants
From sunlight and nutrients
Only significant digestible polysaccharide in the human diet
65
Cellulose
Structural polysaccharide that gives strength to the cell walls of plants
We cannot digest but it is important roughage, swelling with water and moving things along
66
Carbohydrates...
- are often conjugated with (covalently bound to) proteins and lipids
- those pr. and li. On the outside edge form glycolipids and glycoproteins
67
Glycoproteins
Conjugated carbohydrate
| Component of the cell surface coat and mucus...
68
Glycolipids
Conjugated carbohydrate
| Component of cell surface coat
69
Proteoglycan
Conjugated carbohydrate
Cell adhesion; lubrication; supportive filler of some tissues and organs
Have a protein moiety and dominant carbohydrate moiety
70
Moiety
Each component of conjugated molecules
71
Lipid
Hydrophobic organic molecule, usually composed of only C+H+O with a high ratio of hydrogen to oxygen
Less oxidized than carbs and so has more cals/g
72
Fatty acid
Chain of usually 4-24 C atoms with a carboxyl group at one end and a methyl group at the other
Saturated - as much H as possible
Unsaturated - some double covalent bonds / Polyunsaturated - many C=C
Precursor of triglycerides; energy source
73
Essential fatty acids
Must be obtained from the diet b/c we cannot synthesize them
74
Bile acids
Steroids that aid in fat digestion and nutrient absorption
75
Cholesterol
Components of cell membranes; precursor of other steroids
76
Eicosanoids
20-C compounds derived from fatty acid called arachidonic acid
Chemical messengers between cells
Ex: prostaglandins
77
Fat-soluble vitamins
A, D, E and K
| Involved in a variety of functions including blood clotting, wound healing, vision, and calcium absorption
78
Phospholipids
Two fatty acids attached to the glycerol which is attached to other fx groups
Major component of cell membranes; aid in fat digestion
Amphipathic (hydrophilic/hydrophobic)
79
Steroid hormones
Chemical messengers between cells
80
Triglycerides
3-C alcohol (glycerol) linked to 3 fatty acids
Energy storage; thermal insulation; filling space; binding organs together; cushioning organs
a.k.a. Triacylglycerols; "neutral fats"
Formed by dehydration synthesis
81
Describe the connection between trams fats and cardiovascular health
Trams fats pack more tightly together, resist enzymatic breakdown, remain in circulation longer, and have more tendency to deposit in the arteries than saturated and cis -unsaturated fats
82
Amphipathic
Molecule that is Hydrophobic and hydrophilic
83
Prostaglandins
5 of the carbons of an eicosanoid are arranged in a ring
| Signaling roles in inflammation, blood clotting, hormone action, labor contractions, ctrl of blood vessel diameter, etc.
84
Steroid
Lipid with 17 of its carbon atoms arranged in four rings, 3 6-sided rings and a 5-sided
Cholesterol is the precursor to other steroids
85
Define good and bad cholesterol
Bad cholesterol is actually droplets in the blood called lipoproteins, which are a complex of chol, fat, phospholipids, and protein. "Bad" chol is low-density lipoprotein (LDL) w/ high ratio of lipid to protein. "Good" chol is high-density L (HDL) w/ lower ratio of lipid to protein and may help to prevent cardiovascular disease
86
Protein
Polymer of 50+ amino acids
Often amphiphilic
Extreme heat or pH can cause denaturation, making the protein unable to perform its normal function
(SOMEtimes reversible)
87
Amino acid
Central C atom with an amino (-NH3) and a carboxyl (-COOH) group bound to it and an -R group distinct to each amino acid
88
Peptide
Any molecule composed of 2+ amino acids joined by peptide bonds
89
Peptide bond
Formed by dehydration synthesis, joins the amino group of one amino acid to the carboxyl group of the next
Dipeptides
Tripeptides
Oligopeptides(
90
Conformation
3D shape
| Even slight change in conformation of a protein may destroy protein fx
91
Primary structure of proteins
Protein's sequence of amino acids, encoded in genes
92
Secondary structure
Coiled or folded shape held together by hydrogen bonds between the slightly negative C=O group of one peptide bond and the slightly positive N-H group of another some distance away
Alpha helix, beta sheet
93
Tertiary structure of proteins
Further bending and folding of proteins into various globular and fibrous shapes
Hydrophobic radicals associating with each other/ hydrophilic radicals attracted to surrounding water
Van der Waals significant here
Disulfide bridges
94
Quaternary structure of proteins
Association of 2+ polypeptide chains by non-covalent forces such as ionic bonds and hydrophilic/-phobic interactions
95
Prosthetic group
Conjugated proteins have this non-amino acid moiety covalently bound to it
Ex: hemoglobin
In quaternary structure
96
Protein fx: structure
Ex: Keratin, for nails, hair, and skin surface
| Collagen, for deep skin, bones, cartilage, and teeth
97
Protein fx: communication
Some hormones and other cell-to-cell signals, receptors of signals
Ligand: hormone or other molecule that reversible binds to a protein
98
Protein fx: membrane transport
Govern and facilitate concerning this
99
Protein fx: catalysts
Most metabolic pathways of the body are controlled by enzymes, globular proteins that function as catalysts
100
Recognition and protection
Glycoproteins work in immune recognition
101
Protein fx: movement
The base for movement, great and small/ some are "motor proteins"
102
Protein fx: cell adhesion
Bind cells to each other : sperm to egg, immune cells to cancer cells, keeping tissues from falling apart
103
Enzymes
Proteins that function as biological catalysts
| Named by the substance it will act upon (substrate)
104
How are enzymes, like CK-1, CK-2, LDH-1, and LDH-5, used as disease markers?
Enzymes have slightly different forms, isoenzymes. They come in different forms depending on where they are in the body. When that part of the body is diseased, that form of that enzyme increases its presence, which can be tested to come up with a diagnosis.
105
Activation energy
The catalyst lowers the activation energy, the energy required to complete the reaction.
106
Enzyme structure and action
Substrate molecule binds to the enzyme at the active site; they form an enzyme-substrate complex
(lock and key)
Enzyme changes shape a tiny bit to fit the substrate; enzyme breaks the bond and the reaction completes, releasing.
107
Enzyme-substrate specificity
Enzyme can only fit one substrate
108
Cofactors
Circa 2/3 of human enzymes require a non protein partner called a cofactors. Iron, copper, zinc, etc. are inorganic.
109
Coenzymes
organic cofactors usually derived from niacin, riboflavin, and other water-soluble vitamins.
Shuttles the electrons from one substrate to another to finish a process.
110
Metabolic pathway
A chain of reactions with each step usually catalyzed by a different enzyme
111
Nucleotides
Organic compounds with three principle components: single or double C-N ring called a nitrogenous base, a monosaccharide, and 1+ phosphate groups
Ex: ATP
112
ATP (Adenosine triphosphate)
Body's most important energy-transfer molecule
113
ATPases
Specialized enzymes for hydrolyzing the third phosphate, where the energy is stored
114
Think about an argument for the use of steroids for legitimate uses and against the use of steroids for athletic performance enhancement
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