BOLOGY 107 Lecture 4 Outline of Last Lecture I. Macromolecules (cont.)a. Carbohydratesi. What a carbohydrate isii. Functionsb. Lipidsi. What a lipid isii. Fatsiii. Phospholipidsiv. Functionc. SteroidsOutline of Current Lecture II. Macromolecules (cont.)a. Proteinsi. What a protein isii. Functionsiii. Structureb. Nucleic Acidi. What nucleic acid isii. Functioniii. StructureCurrent LectureMacromolecules1)Proteinsa)Comprised of carbon, hydrogen, oxygen, nitrogen, and small amounts of sulferb)Monomer- amino acidi)Formed from an amino group, a carbon, carboxyl, hydrogen, and a side chain (R-group)ii)20 R-groups available(1)Used to classify each amino acid(a)Grouped by acidic, basic, polar, or non-polarc)Polymer- polypeptidei)Formed by dehydration making a peptide bondThese 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.ii)Always attaches to the carboxyl end of a chain(1)Linear chain(2)R-groups react to create a 3-D structured)Functions (only a few listed, there are many)i)Enzymatic(1)Catalyst- speeds the breakdown of moleculesii)Defensive(1)Antibodiesiii)Storageiv)Transportation(1)Provide active transport of molecules through cell membranesv)Hormonal(1)Insulinvi)Receptor(1)Receive neurotransmitters in a synapsevii)Contractile(1)Actin and myosin in a muscleviii) Structural(1)Keratine)Protein structure levelsi)Primary(1)Linear sequence(a)Classified by length and composition(2)Ultimately determine shape and function(a)Drives higher level formationii)Secondary(1)Localized 3-D structure, shown as ribbons or space-filling(a)Hydrogen bonds are formed with the carbon backbones(i)α-helix (right-handed)(ii)β-pleated sheetiii)Tertiary(1)Higher order, shown as ribbons or space-filling(a)Refers to entire polypeptide shape(i)Formed by hydrogen bonding, ionic bonding, hydrophobic grouping, Van Der Waal’s attraction, covalent bondingiv)Quaternary(1)Multiple polypeptides interacting, shown as ribbons usuallyv)Allows for high specificity and 3-D interactionsvi)Single change in primary structure can change the whole proteinvii)Protein folding (naturation(1)Spontaneous, corrected by other proteins(a)Not a directed action(b)If folded wrong, go through denaturation (unfolding) until proper naturation reached(i)Carried out by chaperonins in cell cytoplasym2)Nucleic Acidsa)Formed from carbon, hydrogen, nitrogen, oxygen, and phosphorousb)Monomer- nucleotidei)Nitrogen base, sugar, and a phosphate group(1)Always negativec)Polymer- polynucleotide (DNA and RNA)i)Sugars are linked through phosphodiester bondii)Bases(1)Pyrimidines (one ring)(a)Cytosine, thymine, uracil(2)Purines (two ring)(a)Adenine, guanine(3)Form specific bond(a)Double helix(i)Antiparalleld)Frederick Sangeri)First Nobel Prize(1)Determined the protein sequence for insulinii)Second Nobel Prize(1)First to sequence DNAe)Functioni)Store and transmit information, usually
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