Chapter 2: The Chemistry of Life

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Anatomy & Physiology I

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72 Terms

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Chemistry

The study of matter and energy.

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Matter

Anything that has mass and occupies space, composed of elements.

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Energy

Power to do work.

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Elements

Simplest form of matter. Periodic table of elements—lists all known elements.

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Octet Rule

elements with atomic number less than 20 have their outermost shell hold up to eight electrons.

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Kinetic energy

Stored energy.

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Potential energy

The potential for more energy to be gain.

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Isotopes

varieties of an element that differ only in the number of neutrons; different atomic mass.

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Radioisotopes

unstable isotopes that decay and give off radiation in a process called radioactivity.

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Intense radiation can be ionizing (ionizing radiation)

Examples: UV radiation, X-rays, alpha particles, beta particles, gamma rays.

ejects electrons, destroys molecules, creates free radicals—cause genetic mutations and cancer.

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Some radioisotopes have scientific and medical uses, what are they?

-Dating fossils (carbon-14)
-Diagnostic imaging; Cancer treatment
-Power supply for implants such as cardiac pacemakers

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An ion is….

a charged particle with unequal number of protons and electrons.

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Ionization

transfer of electrons from one atom to another.

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Anion

net negative charge due to gain of electrons.

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Cation

net positive charge due to loss of electrons.

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Ions with opposite charges are….

attracted to each other.

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Electrolytes

Examples: Calcium chloride, Sodium chloride, Potassium chloride.

substances that ionize in water.

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Molecule

composed of two or more atoms united by a chemical bond.

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Compound

molecule composed of two or more different elements.

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Kinds of chemical bonds….

(Attractive forces holding atoms together.)

-Covalent bonds

-Ionic bonds

-Hydrogen bonds

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Single covalent bond

nuclei share 1 pair of electrons.

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Double covalent bond

nuclei share 2 pairs of electrons.

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Cation

a positively charged ion.

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Anion

a negatively charged ion.

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Water is _____ of body weight?

50 to 75%

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Solvency

ability to dissolve other chemicals.

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Hydrophilic

substances dissolve in water; are
polarized or charged. Likes water.

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Hydrophobic

substances do not dissolve in water; are nonpolar or neutral. Does not like water.

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Adhesion

tendency of one substance to cling to another.
Water adheres to membranes reducing friction around organs.

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Cohesion

tendency of molecules from same substance to cling to each other.

-Water is very cohesive due to its hydrogen bonds

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Water has the ability of what?

(Certain type of stability for water)

Thermal stability due to high heat capacity, it doesn’t increase temperature really fast or very slow.

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Chemical reactivity

ability to participate in chemical reactions.

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Acid

◦ Any molecule that releases hydrogen ions (H+)
◦ Increases hydrogen ion concentration in solutions

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Base

◦ Any molecule that can accept hydrogen ions (H+) or releases OH-
◦ Decreases hydrogen ion concentration in solutions

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pH Scale

A measure of hydrogen ion concentration.

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Human Blood is a pH of?

7.4

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Buffers….

-Minimize pH change
-Help maintain stable pH in body fluids

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The body’s most important buffer pairs….

Carbonic acid and bicarbonate.

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Synthesis Reaction or Dehydration synthesis

(Chemical reaction)

formation of a large molecule out of smaller molecules.

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Decomposition Reaction or Hydrolysis

(Chemical reaction)

formation of smaller molecules out of a large molecule.

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Organic compounds are molecules that contain a carbon backbone, essential for life and forming the basis of four major biological macromolecules:

Carbohydrates, lipids, proteins, and nucleic acids.

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These macromolecules are polymers, meaning….

They are large chains built from smaller repeating units called monomers.

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Monosaccharides are the simplest carbohydrates, what are they?

Glucose, galactose, and fructose.

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Disaccharides are….

sugars made of two covalently bonded monosaccharides.

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Three important disaccharides….

Sucrose (table sugar)—glucose + fructose

Lactose (milk sugar)—glucose + galactose

Maltose (sugar in grain products)—glucose + glucose

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Oligosaccharides are….

short chains of 3 or more monosaccharides.

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Polysaccharides are….

long chains of monosaccharides (~50 or more).

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Three important polysaccharides….

Glycogen—energy storage in cells (ex. liver, muscle, brain)

Starch—energy storage in plants; digestible by humans

Cellulose—structural molecule in plants: fiber for humans (indigestible)

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Lipids

Hydrophobic organic molecules with a high ratio of hydrogen to oxygen.

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Five primary types of lipids in the human body….

  • Fatty acids

  • Triglycerides

  • Phospholipids

  • Eicosanoids

  • Steroids

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Fatty Acids, the two types are….

Saturated fatty acids and Unsaturated fatty acids.

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Saturated fatty acids….

Solid at room temperature.
• Single bonds between carbons; saturated with hydrogen
• Animal fats

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Unsaturated fatty acids….

Liquid at room temperature.
• Double bond between one or more neighboring carbons
• Oils: monounsaturated fat (e.g., olive oil);
polyunsaturated fat (e.g., canola oil).
• Mostly from plant origin

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Proteins have three to four levels of complexity:

Insulin
Collagen

Globular proteins; muscular filaments Hemoglobin

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Triglycerides

Each fatty acid covalently bonded to the oxygen atoms of the –OH groups of the
glycerol molecule.

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The negative effects of artificial trans fats….

Trans fats, formed from partially hydrogenated oils, resists enzymatic breakdown in the human body, remain in circulation longer, deposits in the arteries; thus, raises the risk of heart disease.

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Phospholipids

  • Cell membrane structure: Bilayer

  • Hydrophobic and hydrophilic regions, the head being hydrophilic, and the tail being hydrophobic.

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Cholesterol is the “parent” (backbone)….

steroid from which other steroids are synthesized.

- Important for nervous system function and structural integrity of all cell membranes.

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Other steroids include….

Cortisol, progesterone, estrogens, testosterone, and bile acids

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Polymer of amino acids joined by peptide
bonds….

Oligopeptides (10 to15 amino acids)

Polypeptides (larger than 15 amino acids)

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Amino acids have a central carbon with three attachments….

◦ Amino group (-NH2)
◦ Carboxyl group (–COOH)
◦ R (radical) group

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Proteins have three to four levels of complexity:

a) Primary structure, ex. Insulin

b) Secondary structure, ex. Collagen

c) Tertiary structure, ex. Globular proteins; muscular filaments

d) Quaternary structure, ex. Hemoglobin

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Proteins Shape referred to as their….

Conformation

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Conformation is….

  • Unique; crucial to function

  • Proteins can reversibly change conformation to affect function

  • Important examples seen in muscle contraction, enzyme catalysis, membrane channel opening, and so on.

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Denaturation is….

Extreme conformational change that destroys function.

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What can cause permanent (irreversible) denaturation?

Extreme heat or pH.

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Enzymes….

Proteins that function as biological catalysts.
◦ Enzymes act on one or more substrates
◦ Speed up chemical reaction by lowering the activation energy
◦ Permit reactions to occur rapidly at body temperature
◦ Enzymes are not used up in reactions, and are reused.

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Enzymatic Reactions….

Temperature, pH and other factors can change enzyme shape and function
• Optimum pH
• Salivary amylase works best at pH 7.0
• Pepsin in stomach works best at pH 2.0

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Temperature optimum for human enzymes is usually near body temperature of?

(37°C) or (98°F)

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Nucleic Acids….

(Polymers of nucleotides)

• DNA (deoxyribonucleic acid)
• RNA (ribonucleic acid)

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DNA (deoxyribonucleic acid)….

  • Contains millions of nucleotides

  • Constitutes genes involved in protein synthesis

  • Stays in the nucleus

  • 2 strands

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RNA (ribonucleic acid)….

  • 70 to 10,000 nucleotides long

  • Carries out genetic instruction (encoded in DNA) for synthesizing proteins

  • Can leave the nucleus

  • 1 strand