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WKU BIOL 120 - Protein Structure

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BIOL 120 1st Edition Lecture 8Outline of Last Lecture I. Lipids (continued)II. Lipids structure a. phospholipids, glycerol phospholipids, amphipathic III. Proteins key conceptsIV. Structure a. peptide bond, polypeptide, N-terminus, C- Terminus V. Protein functions Outline of Current LectureI. Protein Structurea. denatured, renaturedII. Catalyst and Enzymes a. catalyst, activation energy, enzymesIII. Cell Structure Introa. cell theory, resolution IV. Prokaryotic cells (beginning) a. Plasmids Current LectureI. Protein Structure (hierarchy) These notes represent a detailed interpretation of the professor’s lecture. GradeBuddy is best used as a supplement to your own notes, not as a substitute.1. PrimaryA. unique sequence of amino acids B. Polypeptide properties and function are affected by R group amino acidsC. Single amino acid change affects and alters protein function2. SecondaryA. Folding of primary structure  hydrogen bonds connect the COO- group of one amino acid with the NH3+ group of anotherB. Can bend into either:i. Alpha helicesii. Beta pleated sheets3. Tertiary A. the interaction between R groups or between R groups and the peptidebackbone  bonding secondary structures togetheri. bonded through: hydrogen bonds, hydrophobic interactions, vander Waals interactions, covalent disulfide bonds (two amino acids have thissulfer), and ionic bonds4. Quaternary A. the combination of distinct polypeptide subunits that interact to form asingle structure5. Folding and FunctionA. denatured:(unfolded) protein is unable to function normally. (Quaternary  primary)B. Renaturation: normal folding (primary  Quaternary) C. Molecular chaperones help proteins in cells fold correctly in order to function II. Catalyst and Enzymes1. Catalyst: a substance that lowers the activation energy of a reaction and increases the rate of reaction A. Catalysis is the most fundamental protein functionB. lowers the activation energy of a reaction by lowering the free energy of the transition state  cannot change ∆G and is not consumed C. Activation energy: the amount of free energy required to reach the intermediate condition or transition state i. Reaction rate depends on:1. kinetic energy of the reactants2. concentration of the reactants3. ∆G4. activation energy of the particular reaction 2. Enzymes: protein catalyst that typically catalyze only one reaction A. they bring reactants together in a precise orientation B. they stabilize transition states C. They work by bringing together substrates into a specific position  this stabilizes the transition state and lower the activation energy needed D. Steps of enzyme catalysis1. Initiation 2. Transition state facilitation3. Termination III. Cell Structure1. Cell Theory  All organisms are composed of cells; cells are the basic unit of life; cells arise only from pre-existing cells 2. Size is limited by:A. surface area availableB. TemperatureC. Concentration gradientD. Distance 3. MicroscopesA. most cells are not visible to the naked eyeB. Resolution: minimum distance two points can be apart and still be distinguished as two separate points C. Can use either light microscope or Electron microscope4. Grouping cellsA. Prokaryotes  lack a membrane bound nucleusi. Bacteria and ArchaealB. Eukaryotes  have a membrane bound nucleus and membrane bound organelles i. Eukarya IV. Prokaryotic Cells1. StructureA. All lack a membrane B. Bacteria:a. lack a membrane bound nucleus b. Has a plasma membranec. Posses a single chromosome (nucleoid)i. contains a long strand of DNA and a few supportive proteins d. Has ribosomes, which synthesize proteins e. Stiff cell wallf. Some contain plasmids small, supercoiled, circular DNA molecules 2. Genetic information A. most prokaryotic cells have one supercoiled circular chromosome found in the nucleoid 


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