BOLOGY 107 Lecture 4 Outline of Last Lecture I Macromolecules cont a Carbohydrates i What a carbohydrate is ii Functions b Lipids i What a lipid is ii Fats iii Phospholipids iv Function c Steroids Outline of Current Lecture II Macromolecules cont a Proteins i What a protein is ii Functions iii Structure b Nucleic Acid i What nucleic acid is ii Function iii Structure Current Lecture Macromolecules 1 Proteins a Comprised of carbon hydrogen oxygen nitrogen and small amounts of sulfer b Monomer amino acid i Formed from an amino group a carbon carboxyl hydrogen and a side chain Rgroup ii 20 R groups available 1 Used to classify each amino acid a Grouped by acidic basic polar or non polar c Polymer polypeptide i Formed by dehydration making a peptide bond 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 ii Always attaches to the carboxyl end of a chain 1 Linear chain 2 R groups react to create a 3 D structure d Functions only a few listed there are many i Enzymatic 1 Catalyst speeds the breakdown of molecules ii Defensive 1 Antibodies iii Storage iv Transportation 1 Provide active transport of molecules through cell membranes v Hormonal 1 Insulin vi Receptor 1 Receive neurotransmitters in a synapse vii Contractile 1 Actin and myosin in a muscle viii Structural 1 Keratin e Protein structure levels i Primary 1 Linear sequence a Classified by length and composition 2 Ultimately determine shape and function a Drives higher level formation ii Secondary 1 Localized 3 D structure shown as ribbons or space filling a Hydrogen bonds are formed with the carbon backbones i helix right handed ii pleated sheet iii 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 bonding iv Quaternary 1 Multiple polypeptides interacting shown as ribbons usually v Allows for high specificity and 3 D interactions vi Single change in primary structure can change the whole protein vii 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 cytoplasym 2 Nucleic Acids a Formed from carbon hydrogen nitrogen oxygen and phosphorous b Monomer nucleotide i Nitrogen base sugar and a phosphate group 1 Always negative c Polymer polynucleotide DNA and RNA i Sugars are linked through phosphodiester bond ii Bases 1 Pyrimidines one ring a Cytosine thymine uracil 2 Purines two ring a Adenine guanine 3 Form specific bond a Double helix i Antiparallel d Frederick Sanger i First Nobel Prize 1 Determined the protein sequence for insulin ii Second Nobel Prize 1 First to sequence DNA e Function i Store and transmit information usually genetic ii enzymatic
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