Unit 1 Study Guide: Chapters 1 & 2
Test on August 30, 2013
CHAPTER 1:
Directional term practice
 The umbilicus(belly button) is INFERIOR to the thoracic region.
Superior/inferior

The knee is PROXIMAL to the ankle.
Proximal/distal

The fingers are DISTAL to the shoulder.
Proximal/distal

The shoulders are LATERAL to the breastbone (sternum).
Medial/lateral

The abdominal muscles are ANTERIOR to the gluteal muscles.
Anterior/posterior
Practice your regional anatomy terms, diagrams on page 16
CORRECT YOUR RETURNED QUIZZES and PRACTICE
Homeostasis is: the body’s ability to maintain an optimal internal environment although things are
constantly changing.

What is homeostatic regulation and why is it important to the body? Maintain normal ranges of
temperature, heart rate, blood levels, etc to prevent disease or disability.
 What happens when homeostasis fails? Disease or sickness
FEEDBACK MECHANISM
 Receptor: Collects stimuli from outside and inside the body; special senses and internal receptors for
temperature, blood pressure, etc.
 Control Center: Integrates and make decisions about stimuli collected by receptors; brain and spinal
cord.
 Effector : Acts on information from control center to respond appropriately; muscles or glands.

Positive Feedback Mechanisms: Negate or Enhance original stimulus? If its high, it goes higher; If its
low, it goes lower.
Example in body? Pain, headache, childbirth

Negative Feedback Mechanisms: Negate or Enhance original stimulus? Reverses original stimulus. If
its low, it goes up; If its high, it goes down.
Example in body? Most NORMAL body processes are controlled by negative feedback. Body
temperature, blood sugar.
CHAPTER 2:
Describe atomic structure, including location and charges of subatomic particles.
Nucleus contains Protons (+) and Neutrons (no charge); Electrons (-) surround nucleus
Describe the different types of bonds that atoms form and why bonds are formed.
 Ionic bonds: Transfer of electrons from one atom to another; ion attraction allows them to be pulled
close to one another.

Covalent Bonds: Equal/unequal sharing of electrons between atoms; difficult to separate.

Hydrogen Bonds: important, weak intramolecular bonds that hold structures together.
What is the main difference between inorganic and organic compounds?
INORGANIC: lacks carbon as a central atom, small, diffuses easily through cell membrane.
ORGANIC: contains carbon as a central atom, large, must pass thorugh channels to enter/exit cell.
 What are the important biological inorganic compounds?
Water, gases, some acids and bases, electrolytes.

Describe the properties of water that make it an important inorganic biological molecule?
Universal solvent
Cushion/Protection
Lubricant base
High heat capacity – resists changes in temperature
Participates in many chemical reactions

What are the four major organic macromolecules?
CORRECT AND KNOW YOUR TABLE FROM THE LAST QUIZ!
1. Carbohydrates: what does our body eventually break a glucose molecule into? ATP
2. Lipids: Know the general function of the following lipids:
Triglycerides: ENERGY
Phospholipids: CELL MEMBRANE STRUCTURE
3. Proteins: what 2 categories of proteins does the human body make?
STRUCTURAL
GLOBULAR
Describe the four structures of protein molecules
PRIMARY: Straight chain
SECONDARY: alpha helix or beta-pleated sheet
TERTIARY: alpha or beta chain folded on itself
QUARTENARY: 2 or more tertiary structure held together by central molecule.
What does an amino acid compound look like? What makes each amino acid different from
another? The R group makes each Amino Acid different from another amino acid.
Draw an amino acid below.
What kind of bonds link amino acids together? PEPTIDE BONDS
What kinds of bonds hold the structures of proteins together? HYDROGEN BONDS
4. Nucleic Acids: STUDY TABLE and KNOW STRUCTURE OF NUCLEOTIDE
Enzyme activity

What are enzymes? PROTEINS that act as BIOLOGICAL CATALYSTS.
ALL ENZYMES ARE PROTEINS but NOT ALL PROTEINS ARE ENZYMES

Describe the structure of an enzyme, including the active site. ENZYMES ARE RELIANT ON SHAPE. THE
FOLDING OF THE GLOBULAR PROTEIN, HELD TOGETHER BY HYDROGEN BONDS, PRODUCES AN
ACTIVE SITE (LOCK) THAT A SPECIFIC CHEMICAL WILL FIT INTO (KEY) IN ORDER TO CATALYZE SPECIFIC
CHEMICAL REACTIONS.

What happens when an enzyme is denatured? THE HYDROGEN BONDS ARE BROKEN AND THE
PROTEIN/ENZYME LOSES SHAPE. This means the shape of the active site is lost and the enzyme can
no longer function as designed.

Provide a biological example in the body of proteins being denatured.
High fever is a good human biological example of enzyme denaturation. When we get a fever, the
high body temperature causes functional enzymes to lose their shape and they can no longer
perform important biological functions.