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BGSU BIOL 2050 - Proteins and Nucleic Acids

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BIOL 2050 1nd Edition Lecture 8Outline of Last Lecture I. Macromoleculesa. PolymersII. Carbohydratesa. Sugarsb. StarchIII. Lipidsa. Fatsb. Phospholipidsc. SteroidsOutline of Current Lecture IV. Proteins a. Typesb. StructureV. Nucleic Acidsa. Typesb. StructureCurrent Lecture Proteins- Account for more that 50% of the dry mass of most cells- Many different functionsI. Typesa. Enzymes: selective acceleration of chemical reactionsb. Defensive: protect against diseasec. Storage: storage of amino acidsd. Transport: transport substancesi. Hemoglobine. Hormonal: coordination of organism’s activitiesi. Insulinf. Receptor: response of cell to chemical stimulig. Contractile and Motor: movementi. Actin and myosin contract musclesh. Structural: supportThese 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.i. Keratin in hair, feathers, and other skin appendagesII. Structurea. Polypeptide: unbranched polymers built from the same set of 20 amino acidsb. Amino Acid: organic molecules with carboxyl and amino group http://educationportal.com/cimages/multimages/16/amino_acid_structure.pngi. R Group: what varies from amino acid to amino acidc. Linked by peptide bondsi. Dehydration synthesisd. Structure and Function: sequence of amino acids determines structure which determines functioni. Primary: unique sequence of amino acidsii. Secondary: consists of coils and folds in polypeptide chainsiii. Tertiary: determined by interactions among various side chains (R Groups)1. Interactions include hydrogen bonds, ionic bonds, hydrophobic bonds, and van der Wahls interactions2. Disulfide Bridges: may reinforce structureiv. Quaternary: results when a protein consists of multiple polypeptide chainse. Sickle Cell: blood disorder resulting from a single amino acid substitution f. What determines Protein Structurei. Chemical Conditionsii. Environmental factorsiii. Denaturation: loss of a protein’s native structureg. Chaperonins: protein molecules that assist the proper folding of other proteinsNucleic Acids- Amino acid sequence of a polypeptide is programmed by a unit of inheritance called a geneI. Typesa. Deoxyribonucleic Acid (DNA)i. Provides directions for its own replicationb. Ribonucleic Acid (RNA)II. Structurea. Polynucleotides: nucleic acids are polymersb. Each nucleotide is made of a nitrogenous base, a pentose sugar, and one or more phosphate groupi. Pyrimidines: one ring1. Cytosine, Thymine, Uracilii. Purines: double ring1. Adenine and Guaninec. Sugar Phosphate Backboned. Double Helix and antiparallel i. Two backbones run in opposite 5’ -> 3’ directions from each otherii. Adenine pairs with Thymine or Uraciliii. Guanine pairs with cytosinee. Linear sequence of nucleotides in DNA molecules are passed from parents to


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