BIOL 1411 1st Edition Lecture 3 Outline of Last Lecture I Atomic Structure II Bonding III Chemical Reactions IV Water Outline of Current Lecture I Proteins II Carbohydrates Current Lecture Polymers molecules of proteins Carbohydrates and nucleic acids Monomers make up polymers covalently bonded Macromolecules polymers with molecular weights exceeding 1 000 Isomers molecules that have the same chemical formula but arranged differently Structural isomers differ in how atoms are joined Cis trans isomers involve a double bond between 2 carbon atoms when carbons share 2 pairs of electrons Optical isomers carbon atom has 4 different atoms or groups of atoms bonded Condensation reactions results in formation of covalent bonds between monomers Hydrolysis reactions breakdown of polymers into monomers releases energy I Proteins Proteins polymers made up of 20 amino acids Polypeptide chains un branched polymers of covalently bonded amino acids Disulfide bridge covalent bond helps determine how a polypeptide chain folds 2 cysteines interact 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 Peptide bond carboxyl group of one amino acid reacts with the amino group of another forming bond Primary structure precise sequence of amino acids linear Secondary Structure alpha helix and beta pleated sheet hydrogen bonds Tertiary Structure 3D shape that arises from interactions covalent ionic hydrogen bond or hydrophobic between R groups Quaternary Structure association of 2 or more polypeptides to form the functional protein Chaperones proteins that help when proteins bind to wrong molecules after denaturation or when they are newly made and still unfolded Heat shock proteins general class of stress induced chaperone proteins N terminus starting protein C terminus ending protein Denatured protein is heated the secondary and tertiary structure is broken down if cooled back down the protein returns to normal tertiary structure demonstrating that the info to specify shape is in the primary structure Hydrogen bonds between N H groups on 1 amino acid and C O groups Proteins bond non covalently with other cellular or extracellular molecules to perform their functions Binding is very specific Structure of protein determines function Between protein and other molecules ionic interactions occur between charged R groups 2 non polar groups interact hydrophobically hydrogen bonds form between 2 polar groups II Carbohydrates General formula Cn H2O n Monosaccharaides smallest sugars 3c to 6c Disaccharides 2 monosaccharaides linked by covalent bonds Oligosaccharides 3 20 monosaccharaides Polysaccharides hundreds or thousands of monosaccharaides starch glycogen cellulose
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