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Anatomy/Physiology 1 > Lecture 2 > Flashcards

Lecture 2 Flashcards

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1
Q

Biochemistry

A

The study of the molecules that compose living organisms

Carbohydrates, fates, proteins, and nucleic acids

Useful for understanding cellular structures, basic physiology, nutrition, and health

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2
Q

The Chemistry of Life (Overview)

A
  1. Atoms, Ions and Molecules
  2. Energy and CHemical Reactions
  3. Water and Mixtures (inorganic compound)
  4. Organic compounds
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3
Q

Elements

A

Simplest form of matter with unique chemical properties

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4
Q

Atomic number

A

Number of protons in the nucleus of an atom

Periodic table
-elements arranged by atomic number

24 elements have biological role
-6 elements = 98.5% of body weight
–oxygen, carbon, hydrogen, nitrogen, calcium, and phosphorus

trace elements in minute amounts

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5
Q

Isotopes

A

same chemical behavior, differ in physical behavior

breakdown (decay) to move stable isotope by giving off radiation

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6
Q

Radioisotopes

A

unstable isotopes that give off radiation

every element has at least one radioisotope

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7
Q

Radioactivity

A

radioisotopes decay to stable isotopes releasing radiation

we are all mildly radioactive

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8
Q

Madame Curie

A

First woman to recieve Nobel Prize (1903)

First woman in worldd to receive a Ph.D.
-Coined term radioactivity
-Discovered radioactivity of polonium and radium
-Trained physicians in use of x-rays and pioneered radiation therapy as cancer treatment

Died of radiation poisoning at age 67

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9
Q

Anions

A

atoms that gained electron (net negative charge)

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10
Q

Cation

A

atoms that lost an electron (net positive charge)

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11
Q

Ions with opposite charges are attracted to each other

A
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12
Q

Electrolyte importance

A

-chemical reactivity
-osmotic effects (influence water movement)
-electrical effects on nerve and muscle tissue

Electrolyte balance is one of the most important considerations in patient care

Imbalances have ranging effects from muscle cramps, brittle bones, to coma and cardiac arrest

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13
Q

Molecules

A

two or more atoms held together by a chemical bond
-N2

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14
Q

Compounds

A

molecules composed of two or more different elements
-CO2

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15
Q

Molecular formula

A

shows elements and how many atoms of each are present

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16
Q

Structural formula

A

location of each atom

structural isomers revealed
-molecular and structural formulas on next slide

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17
Q

Isomers

A

molecules with identical molecular formulae but different arrangement of their atoms

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18
Q

Ionic bonds

A

Attraction of oppositeltt charged ions
-the attraction of a cation (+) to an anion (-)

Electron donated by one and recieved by the other
-no sharing of electrons

Weak bond (easily dissociates in water)

Example: sodium chloride

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19
Q

Single Covalent Bond

A

One pair of electrons are shared

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20
Q

Double covalent bonds

A

Two pairs of electrons are shared each C=O bond

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21
Q

Hydrogen bonding in water

A
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22
Q

Energy

A

Capacity to do work, means to move something

all body activities are a form of work

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23
Q

Potential energy (Stored energy)

A

Not doing work at the time

water behind a dam

chemical energy- potential energy stored in the molecular bonds

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24
Q

Kinetic energy - energy of motion

A

energy that is actively doing work

moving water flowing through a dam

heat- kinetic energy of molecular motion

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25
Decompositon Reactions
26
Synthesis Reactions
27
Exchange Reactions
Two molecules exchange atoms or group of atoms - (Reacting molecules can be shuffled around) AB + CD = ABCD = AC + BD
28
Inorganic Compounds
Do not contain C and H as their primary structrual ingredients
29
Water and Mixtures (solutions)
Our body fluids are complex mixtures of chemicals A mixture consists of substances that are physically blended but not chemically combined Mixtures inour bodies contain water Water 50-75% of body weight
30
Solvency
Ability to dissolve other chemicals
31
Solution
Solvent + solute Water = universal solvent
32
Chemical reactivity of water
is the ability to participate in chemical reactions -water ionizes into H+ and OH- -water ionizes other chemicals (acids and salts) -water involved in hydrolysis and dehydration synthesis reactions
33
Solution, Colloid, adn Suspension
34
Acids
is an proton donor (releases H+ ions)
35
Base
is a proton acceptor (acceots H+ ions)
36
pH
equals the negative exponent of the hydrogen ion concentration in a solution measured in mole per liter - a pH of less than 7 is acidic solution (H+ > OH-) - a pH of greater than 7 is a basic solution (OH- > H+) - a pH of 7.0 is neutral pH (H+ = OH-)
37
Buffers
is a mixture of chemicals that resists changes in pH when acid or base is added to the solution -our body uses buffers to prevent change --pH of blood ranges from 7.35 to 7.45 --tremors, paralysis or even death
38
Organic Chemistry
Does contain C and H and usually oxygen as well. Carbon primary structural atom Study of compounds containing carbon 4 categories of carbon compounds -carbohtdrates -lipids (fats) -proteins -nucleotides and nucleic acids
39
Carbon (atomic number of 6)
only 4 valence electrons -binds with other atoms that can provide it with four more electron to fill its valence shell forms long chains, branched molecules and rings -serve as the backbone for organci molecules carries a variety of functional groups
40
Functional groups
atoms attached to carbon backbone determines chemical properties
41
Macromolecules
very large molecule since carbohydrates contain long chains, some organic molecules are gigantic (macromolecules) Ex: startch, proteins, and DNA
42
Polymers (Poly [many])
most macromolecules are polymers molecules made of a repetitivie series of identical or similar subunit called monomers
43
Monomers (Mono [one])
an identical or similar subunit
44
Polymerization
joining monomers to form a polymer
45
Dehydration Synthesis
Monomers covalently bond together to form a polymer with the removal of a water molecule
46
Hydrolysis
Splitting a polymer (lysis) by the addition of a water molecule (hydro) - a covalent bond is broken
47
Carbohydrates
-hydrophilic (water loving) organic molecules Contain carbon, hydrogen, and oxygen in a 1:2:1 ratio -Monosaccharide- simple sugar -polysaccharide - many sugars All digested carbohydrates are converted to glucose and oxidized to make ATP (energy)
48
Monosaccharides
Simple sugars General formula is C6 H12 O6 -isomers --same molecular formila with different structural formulas Major monosaccharide -glucose, galactose and fructose --glucose is bodies most important source of energy "metabolic fuel"
49
Disaccharides
Sugar molecule composed of 2 monosaccharides Major disaccharides -sucrose = table sugar --glucose + fructose -lactose = sugar in milk --glucose + galactose -maltose = grain products --glucose + glucose
50
Polysaccharid
Chains of glucose subunits Starch: energy storage in plants. Glucose based polysacharide manufactured by plants, potatoes, grains. Digestible by human for energy Cellulose: structural molecule of plant cell walls. Fiber in our diet Glycogen: energy storage in animals. Found in liver and muscle tissue. If energy is needed glycogen can be broken down to glucose liver synthesizes after a meal and breaks down between meals.
51
Hydrophobic (water fearing) organic molecule
composed of carbon, hydrogen and oxygen
52
Organic Molecules: Lipids
Five primary types in humans
53
Organic Molecule: Protein
Are the most abundant and important organic molecule A long chain (polymer) of amino acids
54
Amino Acid
Five components of amino acid structure -Central Carbon atom -Hydrogen atom -Amino group (--NH2) -Carboxyl group (--COOH) -Variable side chain or R group 20 amino acids used to make the proteins are identical except for the raidcal (R) groupd properties of amino acid determined by -R group
55
Structure of Amino Acids
H-N-H = Amino group H-C-R = (C is central carbon), (R groups {variable sidechain of one or more atoms}) O=C-OH (Carboxyl group)
56
Primary structure
Sequence of amino acids along length
57
Secondary structure
H bonding causing spiral, coiling or folded effect (alpha helix or pleated sheet shape)
58
Tertiary structure
further coiling and folding bending into globular and fibrous shapes
59
Quaternary structure
final protein shape- several tertiary structures together
60
Complementary Base Pairing
Nitrogenous bases united by hydrogen bonds DNA base pairings -A-T and C-G Law of complementary base pairing -one strand determines base sequence of other
61
Nucleotide Structure for RNA and DNA
DNA= polymer of nucletides Each nucleotide consist of -phosphate group -sugar --ribose (RNA) --deoxyribose (DNA) -nitrogenous base --adenine --guanine --cytosine --thymine (DNA only) --uracil (RNA only)
62
Nucleic Acids
DNA (deoxyribonucleic acid) -double stranded and held together by H bonding -100 million to 1 billion nucleotides long -contains genetic code --cell division, sexual reproduction, protein synthesis RNA (ribonucleic acid) 3 types -transfer RNA, messenger RNA, ribosomal RNA -single stranded -70 to 10,000 nucleotides long -involved in protein synthesis coded for by DNA
63
Overview of ATP production
ATP consumed within 60 seconds Continually replenished
64
Protein Functions
Some Major Protein Functions 1. Support -Structural proteins 2. Movement -Contractile proteins 3. Transport -Transport (carrier) proteins 4. Buffering -Regulation of pH 5. Metabolic Regulation -Enzymes 6. Coordination and Control -Hormones 7. Defense -Antibodies
65
1. Enzymes
Are proteins that speed up a reaction by lowering the activation energy Proteins as biological catalysts -promote rapid reaction rates Substrate acts upon an active site on the enzyme forming a product Some examples of enzymes (Digestive System) -pepsin, trysin, amylase Lowers activation energy = energy needed to get reaction started Control of enzymes: a variety of factors (other than cofactors can effect enzyme performance) -temperature and pH --change shape of enzyme and alter its ability to bind --enzymes vary in optimum pH --salivary amylase works best at pH 7.0 --pepsin works best at pH 2.0 -temperature optimum for human enzymes = body temperature
66
Steps of an enzyme reaction
substrate approaches enzyme molecule substrate binds to active site forming enzyme-substrate complex -highly specific enzyme breaks bonds in substrate reaction products released enzyme repears process over and over
67
Enzymatic reaction steps
1. Enzyme and substrate. Sucrose which is the substrates, an active site opening up and the base sucrase is the enzyme 2. Enzyme-substrate complex 3. Enzyme and reaction products, releasing glucose and fructose
68
Cofactors
nonprotein partners (iron, copper, zinc, magnesium or calcium ions) bind to enzyme and change its shape --essentail to function
69
Coenzymes
organic cofactors derived from water-soluble vitamins (niacin, riboflavin) transfer electrons between enzymes
70
Coenzyme NAD+
as it mediates redox reactions through a transfer of electrons between NAD+ (its oxidized form).
71
Organic Molecules: Nucleotides
Nucleotides: contains 3 components 1. nitrogenous base 2. sugar (monosaccharide) 3. one or more phosphate groups Physiological important nucleotides -ATP = energy carrying molecule -cAMP = activates metabolic pathways -DNA = carries genetic code - RNA = assists with protein synthesis
72
ATP
Adenosine Triphosphate It contains adenine, ribose, and 3 phosphate groups. Its a high energy bond is a covalent bond that stores large amounts of energy (usually involving the attachment of a phosphate group to another molecule = Phosphorylation). When the bond is broken energy is released.

Anatomy/Physiology 1 (3 decks)

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