Organic Molecules: an Overview Organic vs. inorganic molecules What is the difference???

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  • Organic Molecules: an Overview Organic vs. inorganic molecules What is the difference???
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  • CARBON Can form 4 covalent bonds with 4 different elements, can also bond with other C atoms Allows for a diverse number of carbon molecules to be formed Can form long chains of carbon and hydrogen atoms bonded togetherhydrocarbon chain Branch structure Ring structure
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  • Introductory TermsIntroductory Terms Biomolecules = 4 types of organic compounds Monomer = subunits, building blocks of a polymer Example: Lego block Polymer = monomers linked together Example: Lego castle
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  • How do we build and break up organic compounds? 1) Dehydration: Synthesis of a molecule, building 2 monomers are linked together by a covalent bond Water is formed and released
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  • 2) Hydrolysis: Breaking down molecules, going in reverse Water is ADDED Polymers are broken into monomers.
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  • Lipids Different types Structure: Made up of hydrocarbon chains Insoluble in water, mostly nonpolar Functions: Long-term energy storage Chemical messengers (hormones) Insulation Waxesprotection
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  • Lipids 1) Triglycerides Fats Made of Glycerol 3 fatty acids Fatty acid = long hydrocarbon chain and a carboxyl (COOH) group at an end. The hydrocarbon chain gives this molecule its hydrophobic nature Ester compounds (ROR) with many different types/functions Made through a dehydration reaction and involved in hydrolysis reactions.
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  • Lipids Saturated Fat = no double bonds Saturated with hydrogen Unsaturated Fat = double bonds Not saturated with hydrogen Double bond allows a bend in fatty acid chain so the chains cannot pack togetherlow melting point
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  • Lipids 2) Phospholipids Have only 2 fatty acids Instead of 3 rd fatty acid, they have a phosphate group Amphipathic Contain both nonpolar and polar regions Major component of cell membrane
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  • Lipids 3) Steroids Made up of 4 interconnected carbon rings Examples: Cholesterol Testosterone Estrogen
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  • Carbohydrates Some have aldehyde groups (aldoses) and some have ketone groups (ketoses) 5-C (pentose) or 6-C sugars (hexose) Monomers: monosaccharides Functions: Short-term energy storage Pasta dinner before the big race, game, etc. Structural Support ** Glucose, fructose, sucrose, lactose
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  • Carbohydrate Composition Monosaccharides: one sugar, simple sugars Basic formula of CH 2 O Seen mostly as cyclic compounds Quick energy Ex. Glucose, ribose, deoxyribose
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  • Carbohydrate Composition (cont.) Disaccharides: double sugar 2 monosaccharides linked from dehydration reaction Characterized by linkages between monosaccharides Ex. Sucrose (table sugar), lactose
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  • Carbohydrates Polysaccharides Complex carbohydrates 10+ monosaccharides linked together Energy storage Ex. Starch, glycogen
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  • Carbohydrates Structural Polysaccharides 1) Cellulose Major component of plant cell walls Monomer = glucose Cannot be digested by humans Fiber! 2) Chitin Used by arthropods to build exoskeletons Monomer = glucose, differs by a functional group. Cell wall of fungi
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  • Proteins Structure: All proteins are created from unique combinations of 20 different amino acids C,H,O,N Major Functions: Structure (keratin in hair & nails) Contraction/movement (actin & myosin in muscles) Energy Transport (hemoglobin transports oxygen) Signaling (hormones can signal cells to respond) Defense (antibodies) Enzymes in metabolism (speed up chemical reactions by lowering activation energy)
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  • Protein StructureProtein Structure Amino Acids monomers of proteins Contain BOTH carboxyl and amino groups 20 types linked together by amide linkages/peptide linkages through a dehydration reaction. R Groups attached to an amino acid create the differences among the 20 amino acids.
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  • Protein TerminologyProtein Terminology Peptide = 2+ amino acids Polypeptide = Many amino acids linked together. **The amino acid sequence is VERY important for the correct shape and function of a protein !!!
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  • Amino AcidsAmino Acids
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  • Protein StructureProtein Structure 4 Levels of Protein Structure 1)Primary Structure Unique sequence of Aas Determined by genes. Sickle Cell Anemia 1)Secondary Structure 3) Tertiary Structure *4) Quaternary Structure
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  • Proteins Denaturation: Situation where a proteins shape is lost When pH, salt concentration, extreme heat, and/or other environmental factors are altered, the protein may unravel and lose its shape Biologically inactive A change in structure alters function
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  • Diseases Associated with Protein Structural Errors Sickle Cell Anemia Alzheimers
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  • Nucleic AcidsNucleic Acids Functions Information storage Participate in chemical reactions Protein synthesis Enzymes Genetics Monomers nucleotides Examples: DNA, RNA, ATP
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  • Nucleotides Pentose (5-carbon) sugar Phosphate Nitrogenous base **Linked together by.. DEHYDRATION REACTION
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  • Types of Nitrogenous Bases 1)Purines Double ring structure Adenine, Guanine 2)Pyrimidines Single ring structure Cytosine, thymine, uracil
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  • REMEMBER!!! Adenine (A) Thymine (T) AND Guanine (G) Cytosine (C)
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  • DNA vs. RNADNA vs. RNA RNA is single stranded; DNA is double stranded RNA has uracil instead of thymine RNA has ribose sugar, & DNA has deoxyribose sugar. Functions: DNA serves as the genetic code for production of proteins. RNA- DNAs helper
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  • Homework Review Notes pp. 978- 984