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

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 together—hydrocarbon chain  Branch structure  Ring structure

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

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

2) Hydrolysis:  Breaking down molecules, going in reverse  Water is ADDED  Polymers are broken into monomers.

Lipids  Different types  Structure:  Made up of hydrocarbon chains  Insoluble in water, mostly nonpolar  Functions:  Long-term energy storage  Chemical messengers (hormones)  Insulation  Waxes—protection

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.

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 together—low melting point

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

Lipids 3) Steroids  Made up of 4 interconnected carbon rings  Examples:  Cholesterol  Testosterone  Estrogen

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

Carbohydrate Composition  Monosaccharides:  “one sugar,” simple sugars  Basic formula of CH 2 O  Seen mostly as cyclic compounds  Quick energy  Ex. Glucose, ribose, deoxyribose

Carbohydrate Composition (cont.)  Disaccharides:  “double sugar”  2 monosaccharides linked from dehydration reaction  Characterized by linkages between monosaccharides  Ex. Sucrose (“table sugar”), lactose

Carbohydrates  Polysaccharides  Complex carbohydrates  10+ monosaccharides linked together  Energy storage  Ex. Starch, glycogen

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

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)

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.

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 !!!

Amino AcidsAmino Acids

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

Proteins  Denaturation:  Situation where a protein’s 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

Diseases Associated with Protein Structural Errors  Sickle Cell Anemia  Alzheimer’s

Nucleic AcidsNucleic Acids  Functions  Information storage  Participate in chemical reactions  Protein synthesis  Enzymes  Genetics  Monomers  nucleotides Examples: DNA, RNA, ATP

Nucleotides  Pentose (5-carbon) sugar  Phosphate  Nitrogenous base **Linked together by….. DEHYDRATION REACTION

Types of Nitrogenous Bases 1)Purines  Double ring structure  Adenine, Guanine 2)Pyrimidines  Single ring structure  Cytosine, thymine, uracil

REMEMBER!!! Adenine (A)  Thymine (T) AND Guanine (G)  Cytosine (C)

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- DNA’s helper

Homework  Review Notes  pp