Background Assumed for Upper Division Courses:

1. Hierarchical organization of living systems

    SUBATOMIC PARTICLES => ATOMS => SMALL MOLECULES => MACROMOLECULES => MACROMOLECULAR ASSEMBLIES=>CELL ORGANELLES => CELLS => TISSUES => ORGANS => ORGAN SYSTEMS => ORGANISMS
    2. Chemical Bonds
      A. Form so atoms become STABLE = have full outer ELECTRON SHELL
      B. Strong bonds = COVALENT bonds & IONIC bonds
      C. Weak bonds = HYDROGEN bonds, HYDROPHOBIC bonds & Van der Waals forces
        I. POLAR & NONPOLAR covalent bonds
        II. HYDROPHOBIC and HYDROPHILIC molecules
      D. STRONG BONDS exist between atoms & small molecules
        I. CONDENSATION and HYDROLYSIS
        II. require ENZYMES to form & break inside cells
         
      E. WEAK BONDS exist between macromolecules, macromolecular assemblies and within macromolecules
        I. chemical environment within cell causes these to form and break
        II. chemical environment acts through EQUILIBRIUM CONSTANT affect concentrations of REACTANTS and PRODUCTS
       
    3. Functional Groups in Biological Molecules
      A. Acetyl, Amino, Carbonyl, Carboxyl, Hydroxyl, Methyl, Phosphate, Sulfhydryl
      B. recognize FORMULA, POLARITY
      C. SULFHYDRYL common covalent crosslinker within/between polypeptide chains
    4. Water
      A. Importance to living systems
         I. it's everywhere
        II. HYDROGEN BOND formation => solubility, cohesion, specific heat, surface tension,
        III. dissociation => two reactive ions = H+ & OH-
      B. PH = - LOG[H+]
        I. [H+][OH-] = 10-14M
        II. appreciate that pH = very important part of chemical environment w/i cell (cf. 2.E.II, above)
        III. approximate pH ranges for physiological, acid & basic conditions
         
         
    Small Molecules & Macromolecules of the Cell

    1. Small molecules = MONOMERS linked together to form macromolecules = POLYMERS
     
    2. For each of the four types of macromolecules

      A. NAME
      B. nature of MONOMER
      C. RECOGNIZE STRUCTURE of monomer & of polymer
      D. general FUNCTION
      E. general LOCATION w/i cell
      F. GENERAL NATURE of macromolecule -hydrophobic vs. hydrophilic vs. charged vs. neutral under physiological conditions
       
    3. For CARBOHYDRATES
      A. general chemical & structural formulae for MONOSACCHARIDES
        I. HYDROPHILIC & therefore water soluble
      B. polysaccharides = linear or branched
      C. FUNCTIONS of polysaccharide
        I. animal: energy storage = glycogen & structure = chitin
        II. plant: energy storage = starch & structure = cellulose
      D. can be COVALENTLY LINKED TO protein or lipid to form GLYCOPROTEINS or GLYCOLIPIDS
       
    4. LIPIDS
      A. built of FATTY ACID CHAIN
         I. alkyl (CH2) chains
        II. very hydrophobic
         
      B. glycerol w/ three fatty acids = TRIGLYCERIDE
         I. long term energy storage
         
      C. glycerol w/two fatty acids and a phosphate link to an "R" = PHOSPHOLIPID
         I. structural component of cell membranes
        II. AMPHIPATHIC
          a. molecule w/areas of 2 different properties
          b. HYDROPHOBIC fatty acid chains
          c. HYDROPHILIC HEAD (glycerol, phosphate & "R")
           
      D. STEROIDS
        I. Four interconnected carbon rings
        II. Cholesterol: plasma membrane component
        III. Hormones
         
    5. PROTEINS
      A MONOMER = amino acid
        I. general structure of an AMINO ACID
        II. 20 common ones
        III. backbone vs. "R" groups
        IV. classes of "R" groups: nonpolar, neutral polar, acidic polar, basic polar
     
      B. POLYMER = PROTEIN
        I. amino acids linked by PEPTIDE BONDS
     
      C. LEVELS OF ORGANIZATION
        I. PRIMARY = amino acid sequence
        II. SECONDARY = a-helix, b-sheet & random coil
        III. TERTIARY = spatial arrangement of regions of secondary structure
        IV. QUATERNARY = spatial arrangement of polypeptides in multimeric proteins
      D DOMAINS of proteins
        I. each domain = piece of polypeptide w/unique function/structure
        II. each domain from different portion of genome
          a. evolution of gene/protein by movement of these regions of DNA
          b. production of multidomain protein by transcript processing
     
      E. IMPORTANT FEATURE is 3D shape & flexibility which => function

      F. FUNCTIONS w/i cell = "tools" of the cell

        I. receptors, transport channels, motors, enzymes, structural elements, carriers
 
    6. NUCLEIC ACIDS
      A. MONOMER = NUCLEOTIDE
        I. phosphate, sugar & base
        II. four kinds of bases in RNA & in DNA
        III. role of EACH CARBON IN THE SUGAR
        IV. DEOXYRIBOSE vs. RIBOSE
         
      B. POLYMER = NUCLEIC ACID
        I. monomers linked by phosphodiester bond between sugar & phosphate
        II. information "written" in base sequence of the monomers
        III. DNA
          a. 2 molecules hydrogen bonded in a double helix
          b. BASE SEQUENCE of carries genetic information
        IV. RNA
          a. several types
          b. each has specific role in converting genetic information of DNA
          into amino acid sequence of protein
         
Energy, Enzymes and Biological Reactions
 
    1. Spontaneous Reactions & The Laws of Thermodynamics
      A. FIRST LAW & SECOND LAWS OF THERMODYNAMICS
        I. energy cannot be created or destroyed, but converted from one form to another
        II. all systems spontaneously move to their lowest free energy condition (most disordered)
     
      B. Reversible reactions & EQUILIBRIUM CONSTANTS
        I. Keq = [P]/[S] = constant for a given reaction
     
      C. ENDERGONIC and EXERGONIC reactions
        I. ENERGY DIAGRAMS
        II. REACTION COUPLING: energy released from exergonic drive endergonic
    2. ATP = energy currency of the cell

    3. Role of ENZYMES in Biological Reactions

      A. enzymes act on ACTIVATION ENERGY of chemical reactions
      B. Characteristics:
        I. BRIEFLY COMBINE w/S
        II. UNCHANGED after catalyzing reaction of S => P
        III. each catalyzes a SPECIFIC reaction
        IV. SATURATED by high [S] e. many contain COFACTORS
      C. Catalytic Mechanisms
        aI. ACTIVE SITE = location in enzyme at which reaction occurs
        II. transition state bound best in active site
        III. SAME ENZYME CATALYZES BOTH DIRECTIONS OF A REVERSIBLE REACTION
         
      D. Factors Affecting Enzyme Activity
        I. SUBSTRATE CONCENTRATION
        II. INHIBITORS: competitive & noncompetitive
        III. TEMPERATURE & pH
      E. ALLOSTERY: allosteric enzymes have >1 binding site

      F. COVALENT MODIFICATION

      EXTREMELY IMPORTANT CONCEPT
        I. minor chemical modification has major effects on protein activity
        II. common modifiers: Ca+2, PO4, CH3, COCH3
        III. KINASES & PHOSPHATASES
       
    4. RNA-BASED CATALYSIS
      A. RNA splicing & processing
      B. Impact on concepts of evolution of life
       
Nucleic Acid and Protein Synthesis

1. Form of the genetic information = structure of DNA double helix

    A. Single DNA molecule = nucleotide linked by covalent bonds between sugar of one & phosphate of next
    B. BACKBONE of DNA
      I. sugar-phosphate w/base of each nucleotide perpendicular to backbone
      II. POLARIZED; one end has phosphate & other end has sugar
    C. Double helix
      I. two DNA molecules
      II. ANTIPARALLEL = 3' => 5' on one molecule next to 5' => 3' on other
      III. hydrogen bonding between COMPLEMENTARY BASE PAIRS
    D. Knowing sequence of one molecule = TEMPLATE, provides sequence of the other
2. Reproduction of the genetic information = replication of a double helix
    A. SEMICONSERVATIVE
    B. DNA POLYMERASE
    C. Role of complementary base pairing
    D. DISCONTINUOUS on one strand & continuous on the other because 3'=>5' on each molecule
3. Use of the genetic information = protein synthesis
    A. TRANSCRIPTION
      I. part of one DNA molecule = template for mRNA synthesis
      II. 3'=>5'
      III. complementary base pairing

    B. TRANSCRIPT PROCESSING

      I. conversion of TRANSCRIPT into mRNA
        a. removal of INTRONS
        b. addition of cap & poly A tail
        c. transport into cytoplasm
       
    C. TRANSLATION
      I. sequence of events
        a.mRNA binds to SMALL RIBOSOMAL SUBUNIT
        b. LARGE RIBOSOMAL SUBUNIT joins complex
        c. AMINOACYL TRNA SYNTHETASE "charges" each tRNA with amino acid
        d. charged tRNAs join RIBOSOME
        e. peptide bond forms as amino acid released from tRNA
        f. free tRNA leaves ribosome
        g. TERMINATION CODON binds termination factor, not a charged tRNA
        h. complex dissociates, releasing polypeptide
         
      II. genetic code
        a. CODON = 3 nucleotide sequence of mRNA
        b. each codon brings in tRNA bearing only one specific amino acid
        c. ANTICODON = 3 nucleotide sequence of tRNA that base pairs with the codon
         
Specific Features of Cell Structure and Function

1. Biological Membranes

    A. FLUID MOSAIC MODEL
      2D phospholipid bilayer with embedded (INTEGRAL) and associated (PERIPHERAL) proteins

    B. INTEGRAL VS. PERIPHERAL PROTEINS

      I. operationally defined by extraction with hydrophobic or hydrophilic solvents
      II. determined by extent & nature of associations with phospholipids of bilayer

    C. Properties of membranes

      I. asymmetry: phospholipids, proteins & carbohydrates
      II. types of mobility: lateral, rotational & flip-flop

Copyright 1997 Western Oregon University.
Direct suggestions, comments, and questions about this page to Dr. Turner.
Web page construction by Lindsay Turner, Dec., 2001