A&p Chapter 2 Basic Chemistry

Front 1

Matter

Back 1

Anything that occupies space and has mass.

Front 2

Mass

Back 2

The actual amount of matter in an object. It is constant

Front 3

Weight

Back 3

Varies with gravity.
- Weigh is less on a mountain top or in space.

Front 4

States of Matter

Back 4

- Solids
- Liquids
- Gaseous

Front 5

Solids

Back 5

Have definite shape
-bones
-muscles

Front 6

Liquids

Back 6

Have a definite volume but conform in shape to container.
-blood in blood vessels

Front 7

Gases

Back 7

Have neither a definite shape nor definite volume.
-air containing oxygen and carbon dioxide.

Front 8

Energy

Back 8

Contains no matter and does not take up space.
Can be measured only by its effect on matter.
Has the capacity to do work or put matter into motion.
-Kinetic and Potential Energy

Front 9

Kinetic Energy

Back 9

Energy in motion

Front 10

Potential Energy

Back 10

Stored energy

Front 11

Electrical Energy

Back 11

Movement of charged particles.
Ion movement along or across cell membranes.
- Nervous System

Front 12

Mechanical Energy

Back 12

Energy directly used to move matter.
-Motor activity

Front 13

Radiant (electromagnetic) Energy

Back 13

Energy traveling in waves
Visible light, infrared, radio, UV, X-rays.
-Light hitting retina for vision
-UV rays hitting skin for production of Vit. D (used for cognitive and bone formation)- in skin, liver, kidneys.
-Damage of UV rays (skin cancer).

Front 14

Energy Conversion

Back 14

Energy converted from one form to another.
-Heat generated
-All energy conversions in the body produce heat.
EX. Core body temp.

Front 15

Elements

Back 15

Unique substances that cannot be broken down into simpler substances by ordinary chemical methods.
-112 elements
-92 occur in nature

Front 16

What makes up 96% of body weight?

Back 16

-Carbon
-Oxygen
-Nitrogen
-Hydrogen
-Trace amounts of 20 others

Front 17

Elements are made of atoms

Back 17

Each element has its own specific composition of atoms
Gives elements their physical and chemical properties.

Front 18

Atomic Structure

Back 18

Nucleus:
Made up of Protons (+) and Neutrons (neutral)
Accounts for 99.9% of an atoms mass
All atoms are electrically neutral
- (+) and (-) cancel out; number of protons and electrons always equal.

Front 19

Mass number

Back 19

The sum of the masses of its protons and neutrons

Front 20

Isotopes

Back 20

Differ in the number of neutrons.
Nearly all elements have 2 or more isotopes.

Front 21

Radioisotopes

Back 21

Heavier isotopes of elements that are unstable and decompose spontaneously.
-Alpha, Beta particles and Gamma Rays.
Has a half life.
-Iodine 131 used to detect thyroid cancer.
-used in PET scans
Used to treat cancers (Radium 226, Cobalt 60).

Front 22

Atomic Weight

Back 22

The average of the relative weights of all the isotopes of an element.
-Tends to be the mass number of the most abundant isotope.

Front 23

Molecule

Back 23

The combination of 2 or more atoms held together by chemical bonds.

Front 24

Molecule of that element

Back 24

Two or more of the same atom.
EX: H2, or O2

Front 25

Compound

Back 25

2 or more different atoms
Ex: H2O

Front 26

Mixtures

Back 26

Substances composed of 2 or more components that are physically intermixed.
- Solutions
- Colloids
- Suspensions

Front 27

Solutions

Back 27

Homogenous mixtures of components.
- Gases, liquids, or solids
- Transparent (do not scatter light)
- Solutes not visible and do not settle out.
- Water is the body's chief solvent.
- Concentration can be described in terms of %; can also be described in terms of molarity (moles per liter).
ex: Air we breathe, Sea water
Medical solutions
-- Saline solution

-- Glucose solution

Front 28

Solute

Back 28

The particles dissolved in the solvent

Front 29

Molarity

Back 29

A mole of any element or compound is equal to its atomic weight or molecular weight in grams.
Ex: Glucose C6H12O6
6(atomic wt of Carbon) +12(atomic weight of Hydrogen) + 6(atomic weight of Oxygen)=180 gm

Front 30

Avagadro's Number

Back 30

1 mole of any substance always contains the same number of solue particles (6.02 x 10^23)

Front 31

Colloids (emulsions)

Back 31

Heterogenous
Translucent or milky
Solutes still do not settle out
Solutes do not scatter light
Sol-gel transformation
Ex: jello; Cytosol of cells

Front 32

Suspensions

Back 32

Heterogenous
Large, often visible solutes
Solutes settle out
Ex: Sand in water; blood

Front 33

Mixtures Vs. Compounds

Back 33

Mixture:
No chemical bonds, only physically intermixed; can be separated by physical means; some mixtures homogenous, some heterogenous.

Compounds:
Chemical bonds present; can only be separated by chemically breaking bonds; homogenous.

Front 34

Electron Shells

Back 34

- Each shell represents a different energy level.
- Amount depends on its energy level.
- Attroaction between positive nucleus and negatively charged electrons greatest closest of nucleus and decreases with distance from nucleus.
- Each electron shell can hold a specific number of electrons.
--Shell 1 - 2; Shell 2 - max 8;
Shell 3 - Max 18;
Subsequent shells hold larger numbers.
-When the outmost shell of an atom is filled to capacity or contains 8 electrons it is said to be stable.
When the outermost energy level contains fewer than 8 electrons, the atom will tend ot gain, lose, or share electrons

Front 35

Types of chemical bonds:

Back 35

Ionic, Covalent (Polar and Non-Polar) and Hydrogen Bonds

Front 36

Ionic Bonds

Back 36

- Results in the formation of ions which are charged particles.
- Transfer of one or more electrons from one atom to another.

Electron acceptor: Anion
Electron donor: Cation
Most are salts; the + and - charges attract each other to form crystals

Front 37

Cations

Back 37

Positive charge
EX:
Sodium (Na+)- extracellular
Potassium (K+)- intracellular

Front 38

Anions

Back 38

Negative charge
Ex: Chloride (Cl-)
Iodide (I-) - Thyroid gland

Front 39

Covalent Bonds

Back 39

-Shared electrons; each atom is able to fill its outer electron shell at least part of the time.
-Single orbital common to both atoms.

Front 40

Single Covalent Bond

Back 40

When 2 atoms share one pair of electrons

Front 41

Double Covalent Bond

Back 41

Sharing of two pairs of electrons

Front 42

Triple Covalent Bond

Back 42

Sharing of three pairs of electrons

Front 43

Polar Covalent Bond

Back 43

-Unequal sharing of electrons
-Slight negative charge at one end of molecule, slight positive charge at other end.
Ex: H2O

Front 44

Nonpolar Covalent Bond

Back 44

-Equal sharing of electrons
-Charge balanced among atoms
Ex: CO2

Front 45

Hydrogen Bonds

Back 45

-More like attractions rather than true bonds.
-Form when a hydrogen atom, already covalently bonded, is attracted to another atom.
-Commonly seen in water molecules (they create surface tension) Ex; lung fluids (Pluera; avilia)
-Extremely important in binding different parts of large molecules together.
---Proteins -polypeptide chain; has to fold into proper shape
---DNA
-Are easily broken

Front 46

Chemical Reactions

Back 46

Occurs when chemical bonds are formed rearranged, or broken.

Chemical equations:
-Reactants
-Product

Front 47

Patterns of Chemical Reactions consist of:

Back 47

- Synthesis
-Decomposition
- Exchange

Front 48

Synthesis

Back 48

-When atoms or molecules combine to form a larger, more complex molecule.
-Bonds are formed
-Anabolic: Builds up
Ex: The formation of proteins from amino acids

Front 49

Decomposition

Back 49

-When a molecule is broken down into smaller molecules or its constituent atoms.
- Bonds are broken
- Catabolic--to break down
Ex: glycogen broken down to glucose.

Front 50

Exchange or displacement reactions

Back 50

-Involves both synthesis and decomposition.
-Parts of the reactant molecules change partners producing different product molecules
Ex:ATP/glucose...glucose 6-phosphate in cellular metabolism

Front 51

Oxidation-reduction reactions
(Redox)

Back 51

-Decomposition and exchange reactions
-Special type of reaction in that electrons are exchanged between the reactions
-The electron donor is oxidized
-The electron receptor is reduced
Ex; NACL reaction- sodium is oxidized, chloride is reduced.

Front 52

Energy Flow in Chemical Reactions

Back 52

--Exergonic: chemical reactions that release energy
--Catabolic reactions:(decomposition)
--Oxidation reactions:
--Endergonic-reactions: in which energy is aquired thus storing more potential energy in the product than the reactants had
--Anabolic reactions: (synthesis)

Front 53

Factors Affecting Chemical Reactions

Back 53

-Atoms and molecule collisions
-Temperature: Chemical reactions proceed at faster rate with increased temp.
-Particle Size: Smaller particles move faster than larger ones and therefore collide more often.
-Concentration: Higher concentrations produce increased rates of reactions.

Front 54

Carbohydrates

Back 54

-sugars, starches, glycogen, cellulose
-only 2-3% of total body mass
--Function--
Mainly as source for generating ATP in cellular metabolism
-Only a few are used as structural components.
EX: deoxyribose in DNA;
ribose in RNA

Front 55

Simple Sugars

Back 55

--Monosaccharides--
Glucose - brain demands it
Fructose
Galactose
Deoxyribose - DNA
Ribose - RNA

Front 56

Disaccharides

Back 56

--Sucrose= glucose+fructose
(table sugar)
--Lactose= glucose+galactose
(breast milk)
--Maltose= glucose+glucose
(less applications)

Front 57

Polusaccharides

Back 57

-Tens or hundreds of monosacchrides joined by dehydration synthesis
-Glycogen: storage form of glucose in skeletal muscle and liver
-Starch: the main carbohydrate in food
-Cellulose: Not digestible in humans, but used as a source for bulk to aid in movement of food in GI tract (peristalsis).

Front 58

Lipids

Back 58

-18-25% of body mass in lean adults
-Is hydrophobic (fewer polar covalent bonds)
-insoluble in water; thus must be complexed with proteins for transport in blood.
Ex: LDLs, and HDLs

Front 59

Types of Lipids

Back 59

Triclycerides
Phospholipids
Steroids
- Cholesterol
- bile salts
- Vit D
- Adrenocortical hormones
- Sex hormones

Front 60

Triglycerides
(Neutral fats)

Back 60

Fat deposits (in subcutaneous tissue and around organs) protect and insulate body organs, and are the major source of stored energy in the body.

Front 61

Phospholipids

Back 61

Chief components of cell membranes. Participate in the transport of lipids in plasma. Prevalent in nervous tissue.

Front 62

Steroid:
Cholesterol

Back 62

The structural basis for manufacture of all body steroids. A component of cell membranes.

Front 63

Steroid:
Bile salts

Back 63

These breakdown products of cholesterol are released by the liver into the digestive tract, where they aid fat digestion and absorption.

Front 64

Steroid:
Vitamin D

Back 64

A fat-soluble vitamin produced in the skin on exposure to UV radiation. Necessary for normal bone growth and function.

Front 65

Steroid:
Sex hormones

Back 65

Estrogen and progesterone (female hormones) and testosterone (a male hormone) are produced in the gonads. Necessary for normal reproductive function.

Front 66

Steroid:
Adrenocortical hormones

Back 66

Cortisol, a glucocorticoid, is a metabolic hormone necessary for maintaining normal blood glucose levels. Aldosterone helps to regulate salt and water balance of the body by targeting the kidneys.

Front 67

Eiconsanoids

Back 67

group of molecules derived from fatty acids found in all cell membranes. The potent prostaglandins have a diverse effects, including stimulation of uterine contractions, regulation of blood pressure, control of gastrointestinal tract motility, and secretory activity. both prostaglandins and leukotrienes are involved in inflammation. Thromboxanes are powerful vasoconstrictors.

Front 68

Lipoproteins

Back 68

Lipid and protein-based substances that transport fatty acids and cholesterol in the bloodstream. Major varieties are (HDLs) and (LDLs).

Front 69

Amphipathic

Back 69

Phospholipids
(molecules that have both polar and nonpolar parts)

Front 70

Proteins that make up the amino acids:

Back 70

Valine; Leucine; Isoleucine; Methionine; Phenylalanine; Asparagine; Glutamic acide; Glutamine
Histadine; Lysine; Argenine; Aspartic acid; Glycine; Alanine; Serine; Threonine; Tyrosine; Tryptophan; Cystine; Proline

Front 71

There are four levels of protein structural organization:

Back 71

1. Primary
2. Secondary
3. Tertiary
4. Quaternary

Front 72

Primary structure

Back 72

- The unique sequence of amino acids that are linked by covalent peptide bonds to form a polypeptide chain.

Front 73

Secondary structure

Back 73

- The repeated twisting or folding of neighboring amino acids in the polypeptide chain. The shape stabilized by hydrogen bonds.
--Alpha helix
--Beta sheet

Front 74

Tertiary structure

Back 74

-The three dimensional shape of the polypeptide chain.
-The folding is dependent on the function of the protein.
Hydrophobic portions
Hydrophilic portions
Various types of bonds to stabilize structure; molecular chaperones to aid in the folding process

Front 75

Quaternary structure

Back 75

-When a protein has more than 1 polypeptide chain
-The arrangement of the chains to each other
-Variety of bonds to maintain the structure.
Ex: Hemoglobin

Front 76

Collegen

Back 76

Single most abundant protein found in the body; it is responsible for the tensile strength of bones, tendons, and ligaments.

Front 77

Keratin

Back 77

Structural protein of hair and nails and a water-resistant material of skin.

Front 78

Spectrin

Back 78

Internally reinforces and stabilizes the surface membrane of some cells, particularly blood cells.

Front 79

Dystrophin

Back 79

reinforces and stabilizes the surface membrane of muscle cells.

Front 80

Titan

Back 80

helps organize the intracellular structure of muscle cells and accounts for the elasticity of skeletal muscles.

Front 81

Actin and myosin

Back 81

contractile proteins, are found in substantial amounts in muscle cells, where they cause muscle cell shortening (contraction); they also function in cell division in all cell types. Actin is important in intracellular transport, particularly in nerve cells.

Front 82

Catalysis

Back 82

Protein enzymes are essential to virtually every biochemical reaction in the body; they increase the rates of chemical reactions.

Front 83

Transport

Back 83

Hemoglobin transports oxygen in blood, and lipoproteins transport lipids and cholesterol. Other transport proteins in the blood carry iron, hormones, or other substances. Some globular proteins in plasma membranes are in membrane transport (as carriers or channels).

Front 84

Regulation of metabolism

Back 84

Peptide and protein hormones help to regulate metabolic activity, growth, and development.
Ex: growth hormone is an anabolic hormone necessary for optimal growth; insulin helps regulate blood sugar levels

Front 85

Regulation of pH

Back 85

many plasma proteins, such as albumin, function reversibly as acids or bases, thus acting as buffers to prevent wide swings in blood pH.

Front 86

Body defense

Back 86

Antibodies (immunoglobulins) are specialized proteins released by immune cells that recognize and inactivate foreign substances (bacteria, toxins, some viruses).

Front 87

Protein management

Back 87

Molecular chaperons aid folding of new proteins in both healthy and damaged cells and transport of metal ions into and within the cell. They also promote breakdown of damaged proteins.

Front 88

Enzyemes

Back 88

Globular proteins that act as biological catalysts.
They are though of as chemical traffic cops that keep our metabolic pathways flowing.
They can only increase the speed of reactions. Without them, biochemical reactions proceed so slowly that for practical purposes they do not occur at all.

Front 89

Nucleic acids

Back 89

Includes deoxyribonucleic acid DNA
and ribonucleic acid RNa

Front 90

Nucleotide

Back 90

the structural unit of nucleic acids, which consists of a nitrogenous base (adenine, guanine, cytosine, thymine, or uracil), a sugar (ribose or deoxyribose, and a phosphate group.

Front 91

ATP

Back 91

Adenosine triphosphate is the universal energy compound body cells. Some of the energy liberated by the breakdown of glucose and other food funnels is captured in the bond of ATP molecules and transferred via coupled reactions to energy consuming reactions.