Chapter 2 Outline - Basic Chemistry Chapter - For Anatomy & Physiology - Bio136 PDF

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Chapter 2 - Basic Chemistry

I.

CONCEPTS OF MATTER AND ENERGY A.

Matter

1.

B.

States

a.

Solids

b.

Liquids

c.

Gases

Energy

1.

Forms of Energy (when energy is doing work it is called kinetic energy and when it is inactivate or stored it is called potential energy)

a.

Chemical Energy

b.

Electrical Energy

c.

Mechanical Energy

d.

Radiant Energy

2.

II.

Energy from Conversions

COMPOSITION OF MATTER

A.

Elements and Atoms

B.

Atomic Structure

1.

Planetary and Orbital Models of an Atom (check out Fig 2.1 for a model of a typical atom.

2.

Protons (+)

3.

Neurtons (0)

4.

Electrons (-)

5.

Ions are charged atoms, or atoms that have lost or gained electrons

C.

Identifying Elements

1.

Atomic Number (THIS EQUALS THE NUMBER OF PROTONS)

2.

Mass Number (THIS EQUALS THE # P + # N)

3.

Isotopes (SAME # P AND DIFFERENT # N)

III.

MOLECULES AND COMPOUNDS

IV.

CHEMICAL BONDS AND CHEMICAL REACTIONS A.

Bond Formation

1.

Role of Electrons

2.

Types of Chemical Bonds (It is the number of unpaired electrons in the outermost shell that determines the number of bonds an atom can make.)

a.

Ionic Bonds (Figure 2.4 is nice, and Figure 2.5 is a classic example of ionic bonding. CATIONS HAVE A POSITIVE CHARGE (+) AND ANIONS

(-) HAVE A NEGATIVE CHARGE)

b.

Covalent Bonds (Figure 2.5 shows covalent bonding; these are the strongest types of bonds.

There are two types of covalent bonds: POLAR VS. NON-POLAR COVALENT BONDS. These

bonds are based on ELECTRONEGATIVITY or the strength of the attraction of the atoms for electrons. In polar covalent bonds there is an unequal sharing of electron and the molecules are often water soluble and hydrophilic. Water is the most famous example of a molecule with polar covalent bonds. Oxygen atoms are often involved in polar bonds. In non-polar covalent bonds there is an equal sharing of electrons and the molecules are often water insoluble and hydrophobic.)

c.

Hydrogen Bonds (these are the weakest bonds; seen between water molecules)

B.

Patterns of Chemical Reactions (See Figure 2.9 for nice examples of chemical reactions) 1.

Synthesis Reactions

2.

Decomposition Reactions

3.

Exchange Reactions

V.

BIOCHEMISTRY: THE CHEMICAL COMPOSITION OF LIVING MATTER A.

Inorganic Compounds

1.

Water

a.

High Heat Capacity (absorbs and releases large amts of heat)

b.

Polarity/Solvent Properties (universal solvent)

c.

Chemical Reactivity (hydrolysis reactions, dehydration synthesis)

d.

Cushioning (CSF, amniotic fluid)

2.

Salts (easily dissociate in body fluids; Figure 2.10)

3.

Acids and Bases (Figure 2.11, low pH means a large amount of H+, high pH means a small amount of H+.)

a.

Characteristics of Acids (release H+ into solution)

b.

Characteristics of Bases (remove H+ from solution)

c.

pH: Acid-Base Concentrations (buffers: resist changes in pH.)

B.

Organic Compounds (there are four major macromolecules and you should understand the basic composition of each one. You should know the building blocks of each. )

1.

Carbohydrates (Figure 2.12, C n H 2n O n ) a.

Monosaccharides (building blocks)

b.

Disaccharides (Figure 2.13)

c.

Polysaccharides (You should understand the basic difference between starch and glycogen. Polar, H2O soluble and hydrophilic.)

2.

Lipids (C, H and very little O2)

a.

Neutral Fats (triglycerides, saturated vs. unsaturated, non-polar, H2O insoluble and hydrophobic.)

b.

Phospholipids (have a phosphate group, amphipatic)

c.

Steroids (cholesterol is the precursor to all steroids)

3.

Proteins (amino acids are the building blocks, 20 different, differ by their R-groups, Figure 2.15. There are 4 major levels of protein structure: Primary structure: held together with covalent bonds Secondary structure: forming an alpha helix or beta

pleated sheet and held together with hydrogen bonds Teritary structure: forming a 3-D or globular structure and held together with a variety of bonds

Quaternary structure: 2 or more tertiary structures bond together)

a.

Fibrous and Globular Proteins

b.

Enzymes and Enzyme Activity (Catalyst: helps speed up a chemical RXN.)

c.

3 things that can affect a protein’s native or conformational and working shape: temperature, salt concentration and pH. Changing these conditions can denature the protein or make it non-functional.

4.

Nucleic Acids ( DNA and RNA, nucleotides are building blocks, Figure 2.17. Each nucleotide is made up of 3 things: a sugar, nitrogenous base and a PO4 group)

DNA is: double stranded, deoxyribose sugar, A-T, G-C, never leaves the nucleus RNA is : single stranded, ribose sugar, A-U, G-C, can leave nucleus, template for proteins)

5.

Adenosine Triphosphate (ATP) (provides chemical NRG for cells, modified nucleotide, Figure 2.18, AMP + Pi = ATP, high energy bonds between the phosphates.)...