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Organ. Chem. Bio

The Chemistry of Carbon Chapter 3

QuestionAnswer
Macromolecule Large, complex organic molecules made of smaller subunits
Describe some of carbons properties Has four electrons in its outer shell allowing it to bond with four bonds, and can usually bond to single or double bonds.
Functional Groups Groups of atoms with special chemical features that are functionally important.
Isomers Two structures with identical molecular formulas, but different structures and characteristics
Structural isomers Contain the same atoms but in different bonding relationships
Stereoisomers Identical bonding relationships, but the spatial positioning of the atoms differs in the two isomers
Condensation/dehydration Reaction links monomers to form polymers
Monomer Single units
polymers Many units
Hydrolysis reaction Breaks down a polymer into its monomer
Four types of organic molecules and macromolecules 1) Carbs 2)Lipids 3)Proteins 4)Nucleic Acids
Carbohydrates Molecules used primarily for energy that are composed of carbon, hydrogen, oxygen atoms
Monosaccharides Simplest sugars and are the monomers of carbs; most commonly have five or six carbons
Common monosaccharides Glucose, fructose, and galactose
Polysaccharides Long series of monosaccharides linked together to form long polymers; examples: starch and glycogen, cellulose, chitin
Lipids Macromolecule used for energy storage and structural purposes composed predominantly of hydrogen and carbon
Fatty Acids Monosaccharides of lipids; formed by by bonding glycerol
Saturated Fats Lipids in which all carbons are linked by single covalent bonds; solid at room temp; are straight
Unsaturated Fats Lipids in which one or more double bonds are present between carbon molecules; tend to be liquids at room temp; are kinked
Hydrogenation The artificial addition of hydrogen atoms to an unsaturated fat
Phospholipids The major component o the cell membrane; made up of glycerol, 2 fatty acids, and a phosphate group
Phosphate region polar, hydrophilic, head
Fatty acid chains nonpolar, hydrophobic, tail
Proteins Versatile macromolecules that serve as building blocks composed of carbon, hydrogen, oxygen, nitrogen, and small amounts of other elements
Amino acid the monomers of proteins; side-chain (R-group); twenty different types
Peptide/ polypeptide bond long protein chains that can be broken apart by hydrolysis
Four parts of a protein structure Primary, secondary, tertiary, and quaternary
Primary protein structure The sequence of amino acids in the protein and is determined by genes
Secondary Structure Chemical and physical interactions cause folding due to the formation of hydrogen bonds; exhibits repeating patterns
Tertiary structure Complex 3D shape of a polypeptide can involve hydrogen bonding, as well as sulfide bonds and hydrophobic/philic interactions
Quaternary Structure Made up of two or more polypeptides
Five factors promoting protein folding and stability Hydrogen bonds, ionic bonds and other polar interactions, hydrophobic effects, Van der Waals forces, and disulfide bridges
Nucleic Acids Biological macromolecules responsible for the storage, expression, and transmission of genetic information
Nucleotide Monomer of a nucleic acid consisting of pentose sugar, phosphate group, and nitrogenous bases
Created by: ERD2015
 

 



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