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Bio 120 CHP 5 Lecture Notes

by: Kaity Notetaker

Bio 120 CHP 5 Lecture Notes Biology 120

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This set of notes goes over the biological molecules needed to learn for the BIO 120 course!
General Biology
Jennifer J Jenkins
Class Notes
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This 4 page Class Notes was uploaded by Kaity Notetaker on Sunday September 18, 2016. The Class Notes belongs to Biology 120 at Grand Valley State University taught by Jennifer J Jenkins in Fall 2016. Since its upload, it has received 7 views. For similar materials see General Biology in Biology at Grand Valley State University.


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Date Created: 09/18/16
Chapter 5: Structure and Function of Large Biological Molecules I. Introduction  Macromolecules: large molecules made up of many, many atoms bonded together  Some are polymers = many parts  The building blocks of a polymer are called monomer = single part  Building a polymer requires a dehydration reaction (removing water molecule)  Breaking down a polymer requires a hydrolysis reaction (adds water molecule to break) II. Large Biological Molecules – 4 major types a. Carbohydrates  Sugars and polymers of sugar  Molecules made up of CH2O  Multiple hydroxyl group = OH  Carbonyl group, C=O 1. Monosaccharides  3-7 carbons long  Difference between ketone and aldose is depending on where the carbonyl group is located (aldehyde = end)  Glucose can be linear but usually ring shaped  Functions: source of energy, our cells use glucose for ATP  Building blocks for bigger carbohydrates 2. Disaccharides: Carbohydrates made up of 2 monomers linked together  Ex: Maltose, Sucrose  Glyosidic linkage: Disaccharides requires between 2 monomers (covalent bonds form because of dehydration reaction)  Function: source of energy 3. Polysaccharides: Carbohydrates made up of many sugar monomers linked together  Starch: polymer of glucose  Function: energy source  Plants use starch as a form of energy because starches are long living and can be stored easily  Glycogen: polymer of glucose  Located in plants, cell walls  Function: energy source  Animals DON’T store all their energy as glycogen because extra will be stored as fat, which are very efficient as a form of energy storage  Chitin: Polymer made up of modified  glucose monomers  Found in crustaceans and insects (exoskeleton)  And in fungi cell wall b. Lipids: something that has no or little affinity of water (hydrophobic)  Not polymers  Fats (triacylglycerol) carboxyl group  One glycerol and 3 fatty acids  Linkages are called Ester Linkage  Why are fats hydrophobic? They are non-polar covalent bonds so they have no partial charges  Function: Storage form of energy in animals, insulation, cushioning 1. Saturated Fat: Carbons are fully saturated with hydrogen (straight chains packed together tightly) 2. Unsaturated Fat: Carbons are not fully saturated with hydrogen. Presence of carbon double bond produces kinks in the hydrocarbon tail so that the unsaturated fats cannot pack tightly together 3. Trans Fat: (Hydrogenation) Turns unsaturated fats to have a longer shelf life. Elevates “bad cholesterol” (solid a room temperature) 4. Phospholipids  Structure: hydrophilic head (glycerol) and hydrophobic tails (2 fatty acids), phosphate group on top of head.  Amphipathic properties: head attracts to water because phosphate group has a negative charge  Located in cell membrane (bilayer phospholipid), regulates what goes in and out of the cell 5. Steroids (hydrophobic)  Structure: Carbon skeleton made up of 4 fused rings to which function groups are attached  Many functions  Ex: Cholesterol, Pre-cursor (used to make hormones: testosterone, vitamin D, bile salts)  Component of cell membrane (myelin sheath)  Carried in blood by lipid proteins (HDL, LDL)  Difference between good and bad cholesterol?  HDL – takes cholesterol back to liver, removes cholesterol from artery wall  LDL – Cholesterol deposited in artery walls – which can damage walls, block arteries c. Proteins: Polymers of amino acid 1. Amino acid (building blocks of proteins)  Contains a central carbon bonded to an amino group, carboxyl, and hydrogen with a side chain that can vary 2. Peptide bonds (form between amino acids)  Dehydration reaction to form bond  Covalent bond  Where does it form? Carbon between carboxyl group of 1 amino acid and nitrogen between carboxyl group of the 2 ndamino acid  Keeps adding to the right  Proteins are made in ribosomes  Polypeptides have polarity 3. Structure: Complex, unique 3-D shapes  Structure influences function  Creates different shapes – think “knitting”  Primary = amino acid sequence  Secondary = folding or coiling of amino acid chain due to regular hydrogen bond that occurs within the backbone between Hydrogen, Nitrogen, and Oxygen  Tertiary = irregular contortions of the molecule; stabilizes the 3-D structure. This involves bonding between side chains  Quaternary = 2 or more poly peptide chains  More than one string of amino acid  Sickle cell disease/ change of amino acid in hemoglobin 4. Functions of Proteins  Movement of muscle, transportation, structure, communication (signaling & receptor), enzymes, defense (antibodies of immune system)  Digression – denatured: protein changes 3-D shape  Ex: Mad Cow diseases  Infectious agent: protein called a prion 5. Protein Folding  Chaperonin molecules: enable polypeptides to undergo appropriate folding (construct 3-D shape)  Nucleic acids: polymers of nucleotides (single monomer) (DNA&RNA)  Structure: 3 parts  Phosphate group  Pentose sugar (deoxyribose or ribose)  Nitrogenous base  Pyrimidine (cytosine, thymine, uracil (only in RNA))  Purine (adenine, guanine)  DNA AND RNA = double stranded helix  Important in the making of proteins (located in the nucleus)


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