Carbon and the Molecular Diversity of Life
Carbon and the Molecular Diversity of Life Biology 105
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This 4 page Bundle was uploaded by Ashley-Maria Farnen on Tuesday November 10, 2015. The Bundle belongs to Biology 105 at Indiana University of Pennsylvania taught by in Summer 2015. Since its upload, it has received 24 views. For similar materials see Cell Biology in Biology at Indiana University of Pennsylvania.
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Date Created: 11/10/15
Bio Notes 1. Chapter 3-5 – Carbon and the Molecular Diversity of Life a. Biological Molecules Great and Small i. Key Questions 1. How to organism use carbon atoms are decorated with functional groups to build basic molecules of life? 2. What are the categories of building block molecules? 3. What reaction link and unlink building blocks? 4. How are fatty acids, polysaccharides, nucleic acids, and proteins formed? ii. Subunits and Macromolecules 1. Sugars 2. Lipids 3. Amino Acids 4. Nucleotides 5. Polysaccharides 6. Fate and Cholesterol 7. Proteins 8. 9. DNA and RNA iii. Carbon 1. Carbon chains and rings are linked by single and double covalent bonds iv. Carbon Rings 1. Carbon rings can be flat 2. Carbon rings can be “boat” or “chair” v. Chemical Interactions or Molecules 1. Determined By: a. Shape b. Charge distribution c. Interactions with water d. Interactions with other molecules. vi. Functional Groups 1. Small groups of atoms 2. Contribute to the chemical properties of a molecules 3. Usually attached to the carbon backbone. vii. Examples of Functional Groups 1. OH – Hydroxyl 2. C=O – Carbonyl 3. COOH – Carboxyl 4. NH –2Amine 5. SH – Sulfhydryl 6. PO 4 Phosphate viii. Shape to Biomolecules 1. Lipids do not form chains of subunits 2. Proteins, nucleic acids and carbohydrates can form long chains 3. Carbohydrate chains may not be branches. ix. Linking Subunits to Make Macromolecules 1. Macromolecules subunits are linked by removing water – dehydrating condensation x. Breaking Macromolecules 1. Subunits are broken apart by adding water to a bond – Hydrolysis xi. Lipids 1. Contain high levels of chemical energy. 2. Do not dissolve in water 3. Have few polar functional groups 4. Major component of biological membranes xii. Fatty Acids 1. Are amphipathic – contains some polar groups 2. Saturated (no double bonds) or unsaturated (some double bonds) xiii. Health Effects 1. Saturated fats increase cholesterol levels in the blood. 2. Unsaturated fats have less effect on cholesterol levels 3. Omega – 3 fatty acids (from fish and sea weed) inhibit response in blood vessels and joints. xiv. Forming Triglycerides 1. Subunits a. Glycerol b. 3 Fatty acids 2. Linked by condensation reactions xv. Forming Phospholipids 1. Subunits a. Glycerol b. 2 Fatty acids c. “Head” with phosphate group 2. Amphipathic 3. Linked by condensation reactions. xvi. Phospholipids in Membranes 1. Amphipathic structure causes formation of a bilayer. 2. Charges groups associate with water. 3. Hydrophobic tails clump together. xvii. Glycoproteins and Glycolipids 1. Glycoproteins have short chains of sugars attached to proteins. 2. Glycolipids have short chains of sugars attached to lipids. 3. Both found on the exterior surface of cells. xviii. Polypeptides 1. Functions a. Structure and support b. Transport molecules c. Perform chemical reactions as enzymes xix. Amino Acids 1. Subunits of polypeptides 2. 20 different types 3. Structure a. Amino group b. Carboxyl (acid) group c. R group differ xx. Forming of polypeptides 1. Linked by dehydration condensation 2. Bonds are peptide bonds xxi. Protein Shapes 1. Globular – irregular shapes, non-repeating amino acid sequences 2. Fibrous – regular shapes, repeating sequences. xxii. Protein Structure 1. 4 Levels of folding a. Primary structure is sequence of amino acids 2. Secondary – coils or folds of seconds of proteins a. Alpha helix b. Beta sheet c. Stabilized by hydrogen bonds 3. Tertiary a. 3 – dimensional conformation of entire protein b. Stabilized by covalent, hydrogen and ionic bonds 4. Quaternary a. Multiple peptide chains fitted together to make 1 functional protein xxiii. Protein Folding 1. Some proteins fold spontaneously into their correct 3 – dimensional shape 2. Some proteins need chaperone proteins to fold correctly xxiv. Nucleic Acid 1. Functions a. Contains genetic information (DNA and RNA) b. Some nucleotides used for energy storage 2. Structure a. Subunits – nucleotides b. 3 – building blocks for each nucleotide i. Sugar ii. Phosphate iii. Nitrogen Base xxv. Nitrogen Base 1. 2 Types a. Pyrimidines, single sing b. Purines, 2 rings 2. Differ in fictional groups attached to the rings xxvi. Sugar and Phosphate 1. 5 Carbon Sugars a. Ribose in RNA (ribonucleic acid) b. Deoxyribose in DNA (deoxyribonucleic acid) 2. Phosphate groups link nucleotides together. xxvii. Formation of Nucleic Acids 1. Linked by dehydration condensation 2. Bond is called a phosphodiester linkage b. Key Concepts i. 4 Building Blocks – lipids, sugars, amino acids, nucleotides ii. Functional Groups determine chemistry iii. Dehydration reaction link small molecules iv. Protein shape is determined by R – group.
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