Principles of Biology I
Principles of Biology I BIOL 1107
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This 4 page Class Notes was uploaded by Greyson Gutkowski on Thursday September 17, 2015. The Class Notes belongs to BIOL 1107 at University of Connecticut taught by Thomas Abbott in Fall. Since its upload, it has received 26 views. For similar materials see /class/205863/biol-1107-university-of-connecticut in Biological Sciences at University of Connecticut.
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Date Created: 09/17/15
Biol 1107 9409 Ca2 muscle contraction C vs Si Carbon hashigher electro negativity 4 valence electrons can easily bond with itself Si composes most of the earth s crust C02 stable no morphic desire to combine with anything else Plants can utilize C02 however we cannot they have pigments to transform light energy to chemical energy to form glucose from C02 Si is tied up in the earth s mass rather than the atmosphere so it is not readily available to be utilized CARBON Forms linear branched or ring structures Shape defines emergent physical and chemical properties Emergent properties for all mammals endothermal hair lsomers Double bond geometric isomer Minimal number of carbon atoms necessary to create a structural isomer 4 Enantiomers min for a mirror image 4 unique elementsmolecules 9909 Chapter 5 Four classes of molecules are important Why They are the building blocks of life help understand structure and physiology help develop treatments and medicine Living things are composed of cells cells are composed of biological molecules Biological molecules are not alive but they are key to living organisms lnanimate objects are not composed of biological molecules and are there for not alive Prions string of amino acids that can destroy your tissue 0 Act like a living organism however they are a protein 0 Viruses also have features of living things however they are not defined as living Why These biological molecules arrange themselves in a way so that they can create LIFE Polymers and Monomers Polymers are created from monomers through dehydration synthesis Monomers are created from polymers through hydrolysis Carbohydrate Monomer monosaccharide ex glucose ribose galactose fructose sucrose 0 Ribose is linear however when placed in water forms a ring Ex ribose in RNA is a pentose sugar and in the shape of a pentagon Becausepossibly more stable as a ring able to form double bonds stability polar substance hydrophobic vs hydrophilic o Ribose is conserved over different types of substances Polymer polysaccharidedisaccharide 0 Ex Starch glycogen cellulose I Starch storage for plants I Glycogen storage of energy for animals 0 Stored in majority in the liver and skeletal muscles 0 Relationship to insulin insulin regulated the amount of glucose that is circulated in the body lnsulin causes liver cells to release glycogen reserves so that glucose can be used I Cellulose component of plant cells Significance of understanding how monomers form polymers o If you understand how its constructed you can deconstruct the polymer 0 Can form polymers from different monomers with certain emergent properties Lipids Not constructed by putting monomers together Store energy long term They are a flavoring in processed foods Composition 0 Fatty acid chains attached to a glycerol backbone 0 Most stable form is the triglyceride o Hydrophobic tail hydrophilic head I Phospholipid BILAYER Aka cell membrane semipermeable 0 To strengthen add proteins microtubules cholesterol carbohydrates for reinforcement o Phospholipid bilayer allows molecules like oxygen to pass through freely because they are small protein channel is not needed 0 Water molecules can move through although they are polar Movement rate can be increased by aquaporins 0 Large intestine has many aquaporins imbedded in the lining also nephrons in the kidney 91109 Proteins 100000 unique proteins have been determined in a human being 0 Only 20 amino acids monomers I HZN R group COOH H attached to alpha carbon 0 R group variable group 0 Different shapes o Creates different bonding between amino acids peptide bonds 0 Different polarities hydrophobic vs hydrophilic o Acidity o HZN amine group 0 COOH carboxyl group 0 Secondary structure I Beta pleat and alpha helix 0 Tertiary structure I Globular protein formed from big bends formed by disulfide bridges I Gives the protein its first identity 0 Quaternary structure I Results when two or more polypeptide chains form one macromolecule I Collagen3 polypeptides Hemoglobin4 polypeptides o Hemoglobin can hold a maximum of4 oxygen molecules per molecule of hemoglobin 9 each polypeptide has a site to bind to oxygen 0 How does the body get to the oxygen in hemoglobin I Dentaures hemoglobin causing a change in configuration and the release of oxygen I How does the body denature the protein Change in concentration of C02 changes the pH in the blood CO2 H20 carbonic acid change in pH 0 Denaturation I Heat pH salt Nucleic Acids There may be a 6 h nucleotide Monomer nucleotide o Pentose sugar phosphate group nitrogenous base Lymphocyte Macrophage white blood cell that can move between systems very unique 0 Part of the immune system 0 Movement is important because they can move to the wound site to initiate a healing response quickly 91409 Chapter 6 0 Based on our definition of life we are all made up of cells and must be to be considered alive 0 Must have transitional forms to be alive 0 All cells are related by their descent from earlier cells