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TAMU BIOL 111 - Chapter 5

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Review Molecule vs compound Electron shells valence electrons Isotope isomer Covalent Ionic Hydrogen bonds Define acid base Functional Groups Chapter 5 Macromolecules Pages 68 89 Macromolecules Vital to living organisms nucleic acids proteins carbohydrates and lipids Functional groups play key role Formed via covalent bonds linking monomers to form polymers Dehydration Reaction Removing a water molecule for form a bond Hydrolysis Reaction Adds a water molecule breaking a bond MOLECULES Carbohydrates Lipids Proteins Nucleic Acids FUNCTIONS Store energy structural Store energy structural hormones signaling Widely varied Table 5 1 Instructions for building and reproduction Carbohydrates 1 Monosaccharides a monomer a General formula CH2O n b Linear and ring forms c Note numbered carbons d Examples Glucose fructose ribose 2 Disaccharides a 2 monosaccharides linked via glycosidic linkage b Examples i Maltose Glucose Glucose ii Sucrose Glucose fructose iii Lactose glucose galactose 3 Polysaccharides a Polymers of Monosaccharides i Storage Lipids 1 Starch Plant Storage a Amylose Amylopectin 2 Glycogen Animal storage ii Structural 1 Cell Walls a Ex Cellulose i Hydrogen bonds help to hold cellulose together 2 Exoskeletons a Ex Chitin All are hydrophobic 1 FATS a Glycerol covalently attached to 3 fatty acids b Linked via ester linkages c Formed by DEHYDRATION synthesis d Ex Saturated Fat i Every carbon along the string has as many hydrogen bonded to it as possible e Ex Unsaturated Fat i There is a double bond that causes a bend in the molecular shape Therefore the carbons do not have as many hydrogen s bonded to it as possible 2 PHOSPHOLIPIDS a 3 components i Phosphate group Polar ii Glycerol iii 2 fatty acids b 2 layers form cell membranes c forms a cell membrane 3 STEROIDS a 4 carbon rings i Cholestoral Proteins Diverse enzymes transport receptors antibodies and more see Table 5 1 Monomer Amino Acid 20 Amino acids KNOW which amino acids are polar non polar basic or acidic KNOW four levels of protein structure R group makes the 20 different variations Polymers of amino acids AKA peptides Linked via peptide bonds Formed by DEHYDRADTION synthesis Levels of Protein Structure 1 Primary aa sequence 2 Secondary Interaction between backbone atoms a Alpha Helix b Beta Pleated Sheet 3 Tertiary interaction between side chain atoms 4 Quaternary interactions between more than one peptide a Collagen i Green blue and red peptides b Hemogloben i Made up of four different peptides Start of proten wis always considered amino end Denaturation Disrupting protein structure Heat Disrpts h bonds pH disrupts ionic bonds Chemicals00Disrupts ionic S S H bonds Organic solvent nonpolar turns inside out NUCLEIC ACID Function Instructiosn for building and reproduction Monomer Nucleotide o Phosphate group Polar and Negative Charge o Nitrogenous Base 1 ring Pyrimidines Cytosine C Thymine T In DNA Uracil U in RNA 2 rings Purines Adenine and Guanine o Pentose Sugar Ribose or Deoxyribose Deoxyribose in DNA Ribose in RNA Extra oxygen Polynucelotide Polymer of nucleotides Linked via phosphodiester bonds Formed by DEHYDRATION synthesis Directional sequence 5 3 o RNA Single Strand o DNA Double strands antiparalell


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