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Organic Molecules contain Carbon.
Abundant in all living organisms. |
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| Large, complex organic molecules. |
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4 electrons in outer shell (can contain 4 more).
Can have up to 4 bonds (usually single or double).
Can have polar or nonpolar bonds. |
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| Two structures with an identical molecular formula but different structures and characteristics. Structural isomers contain the same atoms but in different bonding relationships. |
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| change in positioning around double bond. |
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| mirror image of another molecule. |
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| Condensation/Dehydration Reaction |
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Definition
"removal" of water.
Links monomers to form polymers. |
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"addition" of water.
Polymers broken down into monomers. |
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| 4 major organic molecules and macromolecules |
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| Carbohydrates, Lipids, Proteins, Nucleic acids |
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Composed predominantly of hydrogen and carbon.
Defining feature - nonpolar thus very insoluble in water. |
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Responsible for te storage, expression and transmission of genetic information.
Two classes (DNA & RNA) |
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Carbon, hydrogen, oxygen, nitrogen and traces of others including sulfur.
Amino acids are the monomers
-Common structure with variable R-group.
-20 amino acids.
-Side-chain determines structure and function. |
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| Simplest sugars, Most common with 5 or 6 Carbons. |
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Glucose and galactose.
Stereoisomers - identical arrangement of bonds, but different arrangement of atoms. |
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Carbohydrates composed of two monosaccharides.
Joined by dehydration or condensation (glycosidic bond).
Broken by hydrolysis.
Examples - sucrose, maltose, lactose |
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Many monosaccharides linked together to for long polymers.
Examples - Energy storage- starch, glycogen. |
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AKA triglycerides or triacylglycerols.
Formed by bonding glycerol to three fatty acids. |
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All carbons are linked by single covalent bonds.
Tend to be solid at room temp. |
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| Fatty Acids (unsaturated) |
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Contain one or more double bonds.
Tend to be liquid at room temp (oils). |
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Amphipathic molecule
-Phosphate region - polar, hydrophilic.
-Fatty acid chains - nonpolar, hydrophobic, tail.
-Form bilayer important in formation of cell membranes. |
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Four interconnected rings of carbon atoms.
Usually not water soluble.
Small different in chemical struct can mean the difference between testosterone and estrogen. |
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Joined by dehydration of condensation reaction.
-Peptide bond.
-Forms polypeptides
-Proteins are made up of 1 or more polypeptides.
Broken apart by hydrolysis. |
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Primary - Amino acid sequence (determined by DNA)
Secondary - Folding into compact structure
-Alpha - helix
-Beta - pleated sheet
Tertiary - further folding into 3D shape.
Quaternary - 2 or more polypeptides. |
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| Proteins with multiple parts. |
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| 5 Factors promoting protein folding and stability |
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Definition
1.Hydrogen bonds - many weak add to overall strong
2.Ionic bonds and polar reactions - different side chain charges may bond together.
3.Hydrophobic effects.
4.Van der Waal's forces - Weak attractions between atoms.
5.Disulfide bridges - Covalent bonds between 2 Cysteine side chains. |
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| Functional domains within Protein structures |
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| Modules in proteins have distinct structure and functions. |
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Deoxyribonucleic acid.
Stores genetic information coded in the sequence of their monomer building blocks. |
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Ribonucleic acid.
Involved in decoding genetic information into instructions for linking together a specific sequence of amin acids to form a polypeptide chain. |
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| An organic molecule that can be used to form larger molecules (polymers) consisting of many repeating units of the monomer. |
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| A large molecule formed by linking many smaller molecules (monomers) together. |
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| Explain the importance of shape in macromolecules and give an example of the consequences of shape changes in molecules |
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| Summarize the interactions involved in protein shape and explain why temperature and pH affect protein shape |
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