Chapter 2: Chemical Level Of Organization PDF
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University of New Brunswick Saint John
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Summary
This document provides an overview of chemical notations for ions and decomposition reactions, along with details about hydrolysis, catabolism, and synthesis reactions. It also discusses metabolic pathways and the importance of enzymes.
Full Transcript
Chemical notations for lons EX : na/na + (lost 1 electron)/na-(gained electron)/ca...
Chemical notations for lons EX : na/na + (lost 1 electron)/na-(gained electron)/ca / (gained 2 electrons) - Decomposition reactions - Hydrolysis/reaction that involves water (adding water to change the elements) catabolism/breaking covalent bonds releases energy so body can use for growth, - movement mortis-body stiff reactions) + reproduction (rigor cause none of these Synthesis reactions/opposite of decomposition assemble larger molecules Into smaller ones - - Dehydration Synthesis/opposite of hydrolysis - remove water from compound - Decomposition and Synthesis are coupled together for equilibrium Activation - energy - the minimum energy required to do reaction - inside the body they use proteins - Enzymes Promote Chemical reactions - lower energy needed - allow reactions to proceed conditions - Metabolic Pathways - Series of reactions that Interlock and require a specific enzyme (birth defects affect these enzymes therefor these reactions) - Metabolites - Substance created or decomposed in our bodys/processed by enzymes /organic nature) and inorganic compounds. Organic in body inorganic - Nutrients - Essential metabolities/organic compounds always contain carbon and hydrogen sometimes oxygen - Macromolecule - large molecules made of nutrients - Monomer-molecule that can be boned to form a polymer (ion by dehydrationSynthesis / hydrolysis to make monomers form polymers - water-makes about 213 of your body-affects all physiological systems up Key : body mostly Se · (becomes acid) · goes ouy) tomucha mostwaterside essa leaving they won't entering or work properly a socitratio Hypervolemic hyponatremia : Increase in body sodium , greater increase in body water - heart failure , liver disease , renal disease - Abuse of MDMA-seizures brain , edema Lubrication - little friction between water sam - changeprotienpresent t issues in heart water friction blood pool molecules - reduces between surfaces exists chemical reactant-water molecules Participate in reactions such as dehydration Synthesis and hydrolysis Water is a compound that dissolves both molecules solutions Inorganic and organic , acting as a solvent in aqueous compound-polar bluenose * water is an inorganic uneven Physiological systems bonds hold ionic inorganic compounds together , and ionization or dissociation occurs when Ions Interact with water molecules. Aqueous solutions , anions and cations form hydration Spheres , attracting water molecules. Hydraulic molecules , like glucose , dissolve strongly in water Electrons Conduct electrical in the body currents , affecting all cells lon concentration in body fluids is regulated by Kidneys , digestive tract , andSkeletal System C end molecules lack covalent bonds organic polar , are nonpolar , lack hydration sphere , co not dissolve , hydrophobic exhibiting fear , of water like fats and oils Regulation of body fluid PH water dissociates into hydrogen and hydroxide ions , can disrupt cell and tissue function , break chemical bonds , regulate body concentration. PH-measure of concentration in body fluids (negative logarithm 0-14) Acidic-below 7 - Contains more Neutral equal to 7 equal numbers - - Alkaline (basic) - above 7 - more PH Scale :.4 7 blood ↑ Normal PH of is 7 35-7 45.. and tissues breaking chemical bonds Damages cells changing shapes of proteins Altering Cellular - - - functions Acidosis = below 7. 35-PH below 7 causes Coma Alkalosis : above 7. 45- PH above 7 8. Causes Skeletal muscle Contractions Buffers-Stabalize PH by removing or replacing hydrogen ions-maintain normal PH body fluids Buffer systems - normal limits of PH-salt related (carbonic acid , Sodium bicarbonate) Organic compounds - Contain C , H , 0 - long chains of C linked with covalent bonds - soluble in water Functional groups - properties of molecule as mes organic Carbs - C , H O. Ex: and starches Sugars M 1 5 % total body weight -. O a - energy resources (we need carbs to survive - contain card Structural Class & Examples Primary Function Remarks Monosaccharides Glucose, Energy source Manufactured in the body and (simple sugars) fructose obtained from food; distributed in body fluids Disaccharides Sucrose, Energy source Sucrose is table sugar, lactose lactose, is in milk, and maltose is malt maltose sugar; all must be broken down to monosaccharides before absorption Polysaccharides Glycogen Glucose storage Glycogen is in animal cells; other starches and cellulose are within or around plant cells monosaccharides Disaccharide Hydrolysis breaks disacharides to monosaccharides Polysaccharides isomers - molecules with same molecular formula , different structures - Important in molecular function Ex : glucose Fructose , Lipids (fat) - C , H O , - C- H ratio - less 0 from carbs with Similar # of carb atoms Contain phosphorus Nitrogen Sulfur - , , EX : Fats , oils , waxes - insoluble in water * Special transport mechanisms for them in blood Lipid Type Examples Primary Functions Remarks Fatty acids Lauric acid Energy sources Absorbed from food or synthesized in cells; transported in the blood Glycerides Monoglycerides, Energy sources, energy Stored in fat deposits; must be diglycerides, storage, insulation, and broken down to fatty acids and triglycerides physical protection glycerol before they can be used as an energy source Eicosanoids Prostaglandins, Chemical messengers Prostaglandins are produced in (see Module 2.16) leukotrienes coordinating local most body tissues cellular. activities Steroids Cholesterol Structural components of All steroids have the same carbon (see Module 2.16) cell membranes, ring framework hormones, digestive secretions in bile Phospholipids, Lecithin Structural components of Derived from fatty acids and glycolipids (a phospholipid) plasma membranes nonlipid components (see Module 2.16) Fatty acids saturated unsaturated Fewer * hydrogens * one double bond onn = monounsaturated I * double = Polyunsaturated Glycerides - monoglyceride (glycerol + 1FA) - Diglyceride (glycerol + 2 FA) - Triglyceride (glycerol + 3 FA) Hydrolysis breaks glycerides into Fatty acids and glycerol - Lipids in the body essential components for all Cells - - Important as energy reserves - Provide twice as much energy as carbs Functions of lipids chemical messengers/components of cellular structures - - structural lipids - Form outer cell membrane and Intracellular membranes * allow separation of different aqueous solutions Eicosanoids ex : Leukotrienes - Produced by cells to Injury or disease Prostaglandins - released by cells to coordinate cellular activities - Powerful- released by damaged tissue stimulates nerve endings -f sensation of pain) Steroids - Large Molecules - 4 Carbon rings Ex: Cholesterol-maintain plasma membranes - cell growth/division Sex hormones - sexual and other metabolic functions estrogen/testosterone Phospholipids and glycolipids - Both are diglycerides Phospholid-linking diglyceride to nonlipid group - - Glycolipid-Carb attached to diglyceride * both structurally related Proteins molecule in body organic - 20 % total body weight - * a essential - Contains HQ N2 ↓. - long chain of amino acids (20 amino acids in body) - 1000 amino acids determines - Functional propertiesTthree-dimensiol Shape Amino acids - same structural components Central carbon attached to 4 groups (H2 Amino Carboxyl R-variable side chain that gives - , , , amino acid chemical properties) positive and of Zero negative charges net charge - , Peptides - Amino acids linked through dehydration Synthesis Covalent bond connects carboxylic acid of amino acid to amino - one group called peptic bond - Dipeptide - Two amino acids linked together Polypeptides Three linked more amino acids together - or - Peptides over 100 amino acids called proteins Formation : Tripeptide formation Primary Structure-sequence of amino acids Secondary structure - bonds form between atoms at different parts of polypeptide chain Ex : Hydrogen bonds - create Simple Spiral (alpha-helix) or flat pleated Sheet (beta Sheet Tertiary Structure - 3-D Shape (coiling / folding) - Interactions from protien/surrounding water molecules R of amino acids in protein groups - Quaternary Structure - Interaction between polypeptide chains forming protein complex Ex : Hemoglobin - 4 polypeptide subunits that form globular protein - Binds oxygen in red blood cells collagen - 3 linear subunits Intertwine , forming fibrous Protein (Strength to tissues) Denaturation Enzymes facilitate most everything that occurs tertiary Change in protein territory Structure Inside the body Active site - or quaternary - - Protein shape changes and function deteriorates - region of enzyme where substrates must bind - occurs under extreme conditions - tertiary or quaternary structure determined by site shape - Body temp above substrates - Acids and bases - Reacts in enzymatic reactions - Fatal from structural proteins and enzymes - Irreparable damage to tissues and organs can occur * structure of Interacting molecules is Important in enzymatic reactions - substrate/enzyme fit in a "lock and key" fashion binds to substrate Shape and charge (Enzyme) Catalyzes 1 type of reaction - - - characteristic - Specificity 1.Substrate binds to active site on enzyme, Process : forming enzyme-substrate complex 2.Substrate binding results in a temporary, reversible change in shape of enzyme 3.Completed product detaches from the active site 4.Enzyme is able to repeat process control of reaction rates - Multiple enzymes in each cell ~ Enzyme is active under conditions - activation or inactivation important for short-term control over reaction rates and pathways. Saturation limit - max rate of reaction Enzyme molecule is cycling through reaction sequence - High-energy compounds - Donate energy to enzymatic reactions to form products - high energy bonds (covalent bonds that release energy when broken Adenosine triphosphate - High energy compound High energy compounds Formation of adenosine triphosphate - Begins with adenosine (adenine/ribose) Adenosine monophosphate bound to a single phosphate - Adenosine cliphosphate (2) - AMP with a second high energy bund to phosphate Adensoine triphosphate (3) - ADP with high energy bond to phosphate ATP allows energy transfer - ATP from ADP is reversible - EnergyStored ATP is released when ATP broken down to ADP - Allows cells to harness energy in one location and release to another. - Provides energy for vital body functions EX : Contraction of muscles Synthesis of Proteins , carbs , fats DNA and RNA are Nucleic Acids Nucleic acids - large organic molecules - composed of H2 & N , P - Two classes - DNA , RNA - Primary function to store/transfer information (Synthesis of protiens) - consists of one or two long chains formed from dehydration Synthesis of subunits (nucleotides Nucleotide components 1. Phosphate group. Pentose 2 (5-carbon) Sugar-dexyribose or ribose 1. base Nitrogenous al Purines - Adenine Guanine , b) Pyrimidines - Cytosine , thymine (DNA only) , Uracil (RNA only) Nucleic acid structure Phosphate and Sugar molecules join via dehydration Synthesis - forms sugar-phosphate backbone with bases for genetic Info a nitrogenous - - sequence of nitrogenous bases carries information for protein Synthesis DNA molecule - nucleotide chains complementary strands - - strands twist around each other to form double helix (Spiral Staircase - Hydrogen bonds and nitrogenous bases hold two strands together complementary base pairs from shapes of bases Adenine- thymine Cytosine Guanine - - - , RNA molecule - single chain of nucleotides - shape and function depend on nucleotides and Interactions between them - Three types : 1. Messenger RNA (MRNA). 2 Transfer RNA (tRNA). 3 Ribosomal RNA (URNA) Comparison of DNA with RNA : Characteristic DNA RNA Sugar Deoxyribose Ribose Nitrogenous bases Adenine (A), guanine (G), Adenine, guanine, cytosine, cytosine (C), thymine (T) uracil (U) Number of Always more than 45 million Varies from fewer than 100 to nucleotides in about 50,000 typical molecule Molecular shape Paired strands coiled in a double Varies with hydrogen bonding helix along the length of the strand of each of the three main types (mRNA, tRNA, rRNA) Function Stores genetic information that Performs protein synthesis as controls protein synthesis directed by DNA