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Biology 107, Week One of Notes on Ch. 5

by: Alyse Bailey

Biology 107, Week One of Notes on Ch. 5 Bio 107

Marketplace > Washington State University > Biology > Bio 107 > Biology 107 Week One of Notes on Ch 5
Alyse Bailey
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These notes cover all of the key points from the textbook for the week! Simplified for easy digestion and clear focus. If you don't have time to read the entire chapter, don't worry! I already di...
William Davis
Class Notes




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This 18 page Class Notes was uploaded by Alyse Bailey on Monday January 18, 2016. The Class Notes belongs to Bio 107 at Washington State University taught by William Davis in Fall. Since its upload, it has received 15 views. For similar materials see Biology in Biology at Washington State University.


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Date Created: 01/18/16
Chapter 5 The Structure and Function of Large Biological Molecules 5.1 Macromolecules are polymers, built from monomers  Macromolecules o Consist of carbs, proteins, fats o  Polymer o Long molecule consisting of many similar or identical building blocks linked by covalent bonds (like a train of cars) o Carbs o Proteins o Nucleic acids o  Monomers o Repeating units (like the cars that make up the train)  Enzymes o Specialized macromolecules that speed up chemical reactions  Dehydration Reaction o Two molecules are covalently bonded with the loss of a water molecule o  Hydrolysis o This is how polymers are dissembled to monomer o Is essentially the reverse of dehydration reaction o Example: digestion in our bodies o 5.2 Carbohydrates serve as fuel and building material  Carbohydrates  o Sugars and polymers of sugars o Monosaccharides (simple sugars)  Glucose C2H12O6 for example  If it ends in –ose it’s a sugar  Two types  Aldose (Aldehyde sugar) o Carbonyl group at the end of the skeleton  Ketoses (Ketone sugars) o Carbonyl group within carbon skeleton o Disaccharides (double sugars)  Two monosaccharides joined by glyosidic linkage  Glyosidic linkage  Covalent bond formed by a dehydration reaction   Polysaccharides o Macromolecules, polymers with a few hundred to a few thousand monosaccharides joined by glyosidic linkages  Structural  Cellulose o Polymer of glucose o Mostly just pants because it is hard to find enzymes to digest it – cows can o in cotton and paper o “insoluble fiber”  Storage  Plants store starch in plastids, which include chloroplasts  Potatoes o Amylose o Amylopectin – complex starch o Glycogen – branched and able to be used easily  Alpha and beta  Concern for low carb diets because you run out of glycogen for energy  Chitin  Carb used by arthropods to build their exoskeleton  Found in fungi for their outer structure  Nitrogen –containing appendage 5.3 Lipids are a diverse group of hydrophobic molecules  NOT included in polymers  NOT big enough to be considered macromolecules  Mix poorly with water o Fats  Two kinds of smaller molecules:  Glycerol – alcohol   Fatty acids – long carbon skeleton 16-18 carbons in length  Hydrophobic – separate from water because the water molecules hydrogen bond to one another and exclude the fats  Triacylglycerol o 3 fatty acids linked to one glycerol molecule that is formed when they are joined to the molecule by a ester linkage – bond formed by dehydration reaction between hydroxyl group and a carboxyl group o  Saturated fat - No double bonds between carbon atoms composing a chain, hydrogen is free to saturate the structure - Tend to be solid at room temp. - Animal fats  Unsaturated Fat o One or more double bonds with one fewer hydrogen atom on each double-bonded carbon o o Oils – plants and fish  Fats o Used for energy storage, body insulation o  Phospholipids o Constitute cell membranes o Two fatty acids attacked to glycerol rather than three in lipids o 3 hydroxyl group is attached phosphate group o When added to water they self-assemble into double-layered structures “bilayers” shielding their hydrophobic portions from water   Steroids o Lipids characterized by a carbon skeleton consisting of four fused rings o Cholesterol  A type of steroid that is crucial in animals  Component of animal cell membranes and the precursor for other steroids and hormones to synthesize  5.4 Proteins include a diversity of structures, resulting in a wide range of functions 1. “PRIMARY” THE MOST IMPORTANT IN OUR BODIES a. Proteins account for more than 50% of the dry mass of most cells and instrumental in everything that we do b. Chemical reactions c. Transport d. Defense e. Storage f. Cellular communication g. Movement h. Structural support 2. Life would not be possible without enzymatic proteins that regulate metabolism a. Catalysts i. Chemical agents that selectively speed up chemical reactions without being consumed by the reaction ii. Like a workhorse iii. iv. Made of 20 amino acids linked in unbranched polymers v. Peptide bond 1. Bond between amino acids 2. Polypeptides 3. Protein is a biological functional molecule made of one or more polypeptides folded and coiled into a specific three dimensional structure b. Amino Acid Monomers i. Amino acid 1. Organic molecule with both an amino group and a carboxyl group a. Alpha carbon b. Amino group c. Carboxyl group d. Side chain (R group) e. c. Polypeptides (Amino Acid Polymers) i. Two amino acids positioned so that the carboxyl group of one is adjacent to the amino group of the other ii. They become joined by a dehydration reaction, removing a water molecule iii. The resulting covalent bond is a peptide bond iv. d. Protein Structure and Function i. Function is based on the amino acid sequence ii. When a cell synthesizes a polypeptide, the chain may fold simultaneously, assuming the functional structure for that protein iii. There are four levels of protein structure 1. Primary a. Linear chain of amino acids b. 2. Secondary a. Regions stabilized by hydrogen bonds between atoms of the polypeptide backbone b. c. Alpha helix i. Coil by hydrogen binding between every 4 amino acid ii. Hair has a helix structure d. Beta pleated sheet i. Two or more segments of polypeptide chain lying side by side connected by hydrogen bonds 3. Tertiary a. Three dimensional shape stabilized by interactions between side chains b. c. Hydrophobic interaction i. Exclusion of nonpolar substances by water molecules d. Disulfide bridges i. Covalent bonds that reinforce the structure 4. quaternary a. Association of two or more polypeptides b. c. Collagen and hemoglobin iv. Sickle cell disease 1. Inherited blood disease, caused by substitution of one amino acid(valine) for the normal one (glutamic acid) at a particular positon in the primary structure of hemoglobin – carries oxygen to the red blood cells 2. 3. Denaturation a. Protein gets unraveled and loses native shape and becomes biologically inactive b. 4. Protein folding in the cell a. Chaperonins i. Crucial to the folding process, they assist in the proper folding of other proteins ii. Misfolding can cause serious problems iii. iv. X-ray Crystallography 1. Determines 3-D structure of many proteins 2. Help understand protein structure and function 5.5 Nucleic acids store, transmit, and help express hereditary information o Genes  Consist of DNA, which belong to nucleic acids  Nucleic Acids  Polymers made of monomers called nucleotides o Role of Nucleic Acids  Deoxyribonucleic Acid(DNA)   Sugar in DNA o Lacks and oxygen atom on the 2 carbon ring  Ribonucleic Acid (RNA)   Ribose – sugar in RNA  Gene Expression  DNA directions to for replication o Directs RNA synthesis o RNA controls protein synthesis o  Polynucleotides  Nucleic acids as macromolecules that exist as polymers  Monomers called nucleotides  Nucleotides o 1. Five-carbon sugar molecule (pentose) o 2. Nitrogen Containing base o 3. One or more phosphate groups  o Nitrogenous Bases  Pyrimidine – one six-membered ring of carbon and nitrogen atoms  Cytosine - DNA and RNA  Thymine- DNA ONLY  Uracil - RNA ONLY  Purines – larger, six membered ring fused to five-membered ring  Adenine – DNA and RNA  Guanine – DNA and RNA o Nucleotide Polymers  Dehydration reaction to from sugar phosphate backbone  5’ on one side and 3’ on the other o DNA  Two polynucleotides or “strands” that wind into a double helix  They run antiparallel like a divided highway  Held together by hydrogen bonds between paired bases  Adenine – Thymine  Guanine – Cytosine  Two strands of the double helix are complimentary o RNA  Exists as a single strands  Adenine – Uracil  Thymine is NOT present in RNA o 5.6 Genomics and proteomics have transformed biological inquiry and applications o Genomics o Large sets of genes analyzed and compared to other species o Proteomics  Analysis of large sets of proteins and sequences o Helped understand evolution o


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