NS Midterm Outline
Thanks to Professor Busher for this outline. Good luck all!
NS201 – Biological Science – Midterm Exam,
OUTLINE
I. The philosophy of science and nature of biology
A. Naturalistic vs. Vitalistic philosophy
B. Epistemology in science
C. Methodology in science
1. Data model loop
2. Hypothetico-deductive method
3. Characteristics of a “good” theory
D. Biology and the concept of emergent properties
II. Review of the Darwinian Model of Evolution
A. The evolutionary paradigm
B. The mechanism of evolution
1. Natural Selection
C. Evidence for evolution
D. The connection between evolution and this course
III. The characteristics of life
A. Life as an emergent property
B. Laboratory #1 as an illustration of the characteristics of life
1. Response to stimuli in crayfish
2. Territoriality in crayfish
VI. Review of general chemistry
A. Atomic structure
1. Atomic number and atomic particles
2. Valence electrons and valence number
3. The representative elements on the periodic table
4. Electron configuration
5. Attraction of electrons by atoms and electronegativity
6. Ions
7. Electronegativity and bond type
a. Electronegativity scale = 0.7 – 4.0
b. Differences in electronegativity between atoms can determine bond type
c. Ionic bonds (electrostatic attractions) EN difference greater than 1.7
1. Complete transfer of electron(s) creates ions
2. Oppositely charged ions attract and form an ionic substance
3. Usually between metals and non-metals
d. Covalent bonds: EN difference 0.0 – 1.7
1. Sharing of valence electrons
2. Sharing may be equal or unequal
3. Non-polar covalent bonds – equal sharing of electrons
a. EN difference = 0.0 – 0.7
b. Example is hydrogen bonded to carbon
4. Polar covalent bonds – unequal sharing of electrons
a. EN difference = 0.7 – 1.7
b. Example is hydrogen bonded to oxygen
E. Hydrogen bonds – between polar molecules
1. Hydrogen is polar covalently bonded to a strong electronegative atom (oxygen, nitrogen)
2. Hydrogen (with a slight positive charge) is attracted to a negatively charged atom in another molecule
3. Relatively low energy attraction
4. First described by Linus Pauling
V. Characteristics of Water
A. Formation of one water molecule – polar bonds and polar molecule
B. Water and the hydrogen bond – between water molecules
C. State change graph of water (ice-liquid-gas)
1. Heat of fusion (80cal/gr)
2. Specific heat of liquid (1cal/gr/°C)
3. Heat of vaporization (540 cal/gr)
4. The physical state and hydrogen bonding
D. Cohesion and adhesion of water
E. General idea of pH scale and water
F. Water and plant adaptations – lab #2
G. Plant adaptations to drought
VI. Origin of Life on Earth
A. Traditional spontaneous generation of large organisms
1. Macroscopic organisms from abiotic matter
2. Vitalistic concept
3. Disproved by Redi
B. Traditional spontaneous generation of microscopic organisms
1. Anton van Leeuwenhoek and microscopic organisms
2. Needhan-Spallanzani debate
3. Louis Pasteur and the “ultimate” experiment
4. Biogenic law – Life from life
C. A special case of spontaneous generation – Chemical Evolution
1. Haldane-Oparin Hypothesis/ Primordial Sea Hypothesis
a. Life originated in warm nutrient rich ancient oceans
b. Earth’s atmosphere 4.5 billion years ago was reducing – no free molecular oxygen
c. Energy was available from lightning, thermal vents, volcanic activity
2. Miller-Urey experiment
a. Organic monomers could be produced in a reducing atmosphere
b. Precursors of life
c. Simple moleculesàorganic monomersàorganic polymers à protocells(protobionts) à?life?
3. Panspermia – life from space – another possible view?
4. Life originated 3.5-3.8 billion years ago when conditions on Earth were very different from the current Earth
VII. The first organic molecules – How to build a living cell
A. Hydrocarbons
1. Characteristics
a. Dull, repetitive, non-polar, hydrophobic, low chemical reactivity
b. Good foundation for building a cell
c. Saturated vs. unsaturated Hydrocarbons
B. Functional groups – Radicals
1. Add polarity and/or unsaturation to hydrocarbons
2. Higher chemical reactivity
3. Hydrophilic
4. Replace a hydrogen(s) in a hydrocarbon with a radical(s) to make organic monomers
5. Review and know the functional groups
C. Lipids (C, H, O,) some have P and N
1. Lipid characteristics:
a. non-polar
b. hydrophobic
c. some are amphipathic
d. diverse groups of molecules
2. Fats and oils
a. monomers are glycerol and fatty acids
b. Fatty acids may be saturated or unsaturated
c. Fatty acids connected to glycerol by an ester bond
3. Phospholipids
a. monomers are glycerol, fatty acids and a phosphate group
b. molecule is amphipathic (polar and non-polar/hydrophilic and
hydrophobic)
c. major component of cell membranes
d. Danielli-Davson vs. Singer Nicolson models
4. Steroids
a. three 6C rings and one 5C ring.
b. very stable, generally non-polar
c. Testosterone, Estradiol, Cholesterol are examples
d. Function as hormones
5. Isoprenoids
a. vitamin A is an isoprenoid
b. carotenoids, which make carrots orange, are isopreoids
c. Isoprenoids and fall foliage
VIII. Membranes and transport (review chapter 5 and lab 3)
A. Membrane structure – a double layer of phospholipids
1. Models
a. Davson-Danielli
b. Singer-Nicholson Fluid Mosaic model
2. Membrane structure allows transport of materials
a. Integral proteins and material transport
3. Membrane is fluid and allows movement of proteins and phospholipids
within the membrane
2. Lab. #3 Movement of materials across a membrane
B. Types of transport
1. Passive Transport
a. Always is with a concentration gradient: High conc. àLow
conc.
b. No cellular energy is expended in the transport.
c. Examples: Diffusion of a gas in the air, smoke in a room…
d. Osmosis - Water movement across a membrane (High àlow)
1. Water movement is always from a hypotonic towards a
hypertonic solution
2. Hypertonic = high solute, low solvent (water)
3. Isotonic = equal solute and solvent (water)
4. Hypotonic = Low solute, high solvent (water)
5. Remember the lab we did on this – lab #3.
e. Facilitated diffusion – diffusion across the cell membrane
through protein channels
2. Active transport
a. Always against a concentration gradient (Low à high)
b. Cellular energy is expended during transport
c. Examples: Na+ - K+ pump, Proton Pump
IX. Other Biological Molecules
A. Proteins – Control molecules (C,H,O,N,S)
1. Monomer is the amino acid - amphoteric molecule (acid and a base)
2. 20 different amino acids – side group is what makes them different
3. Amino acids bond together by covalent bond = peptide bond
4. Bond forms by dehydration (condensation) reaction (removal of water)
5. Bonding of amino acids creates a polymer called a polypeptide
6. The polypeptide assumes up to four additional structures to be a functional protein
7. Protein structures:
a. Primary – amino acid sequence
b. Secondary – alpha helix (Linus Pauling) and Beta Pleated sheet
c. Tertiary – Globular form – disulfide bonds and hydrogen bonds
d. Quaternary – between more than one protein (electrostatic forces)
e. Review examples of protein structures
8. Functional groups of proteins – what do proteins do?
9. Enzyme activity – review lab #4 – Catechol to Benzoquinone mediated by catechol oxidase (enzyme).
10. Enzyme activity and environmental conditions
a. Temperature and pH can denature enzymes
b. Temperature and pH can alter the active site by denaturing the enzyme
c. Enzymes and the lock and key model of activity
Note: Take a moment to review the objective and organization of the labs. Review your lab notes and the results from the lab experiments.


