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specific groups of atoms within a molecule that are responsible for the chemical reactions of that molecule. |
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4 structures composed of C, H, with little O; functioning in signaling; |
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Simple sugars are able to be absorbed better because |
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they can be easily crossed into the blood stream. |
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humans tend to have saturated fatty acids; the tails tend to be straight; triglyceride is solid at room temperature |
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double bonds are present (kinky); some carbons do not have a full set of H; tends to be a liquid at room temperature; plants will have more unsaturated fatty acids. |
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unsaturated, but structured so it's solid at room temperature(it packs well: ex. margarine); increases risk of heart disease; stable at room temperature and easy to make |
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Used for plasma membranes; composed of a head and 2 fatty acid tails; head is composed of Glycerol, Phosphate and Choline. Tails are uncharged-nonpolar-hydrophobic; the head is hydrophillic and polar; can form phospholipid bilayers between a cell and the external enviornment. |
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composed of carbon, hydrogen, and very little oxygen; hydrophobic because of the proportion of C+H to O; non polar |
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1. Triglycerides 2. Sterols 3. Phospholipids |
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- creating your cell membranes. - storing energy. -insulation. -sterols are involved in signaling. -light energy capture. -water repellent function |
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fats and oils; used for energy storage and insulation; composed of a glycerol head and three fatty acid tails that are saturated or unsaturated. |
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2 sugar rings covalently bonded together; "complex carbohydrates" |
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3 or more sugar rings covalently bonded together "complex carbohydrates" |
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Examples of Polysaccharides |
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1. Glycogen 2. Cellulose 3. Starch (ex. Fiber) |
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carbohydrate composed of 1 sugar ring by itself. "simple sugar" |
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composed of C, H, and O; Hydrophillic (the high proportion of oxygen allows them to hydrogen bond) |
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Functions of Carbohydrates |
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-store energy; -carry energy; -structure to cells; -high amount of carbon used to generate carbon skeletons for new molecules |
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proteins whose function is to help other proteins fold; has a favorable bonding environment that helps other proteins fold. |
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dictate if a protein can interact with another protein or molecule |
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the sequence of amino acids linked by a peptide bond in a chain |
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two types: alphahelix( squiggly line) or a beta (accordion) |
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the 3D shape of one polypeptide (amino acid); involves hydrogen bonds, ionic bonds, covalent bonds, and nonpolar forces by the way of R Groups. |
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the 3D shape of more than 1 protein. |
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can create a covalent bond. SH can form covalent bonds with another SH. |
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When You Look At A Amino Acid: |
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1. Charged/ Uncharged (Polar/ Nonpolar) 2. Large/ Small 3. Hydrophillic/ Hydrophobic |
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Peptitde bonds form through |
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Four Levels of Protein Folding |
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Primary Structure: chains of amino acids linked by a peptide bond. Secondary Structure: helixes or beta pleated sheets Tertiary Structure: 3D Shape of 1 protein Quaternary Structure: 3D Structure of a protein complex |
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COO- is the same in every group. The difference is the |
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give each amino acid a different function/ property; important for protein folding; typically shown in a box in a reaction chain. |
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Fights infections; built by the immune systems |
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Cells receive and transmit |
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Cytoskeleton= protein scaffold that gives structure to cells |
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helps decide what genes are ON or OFF |
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Two molecules come together and a water molecule (H2O) is produced. Two monomers are conjoined by covalent bonds. |
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Water is used and a polymer is split into pieces. |
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Are composed of amino acids linked by peptide bonds (a specialized form of covalent bonds). "workhorses of the cell" |
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Proteins that do chemical reactions that support life; initiate and accelerate |
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Where the layout is CLEARLY different |
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whenever the molecules are mirror images of each other. Referred to as D&L. |
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Also known as optical isomer. Example: L Form= sudafed (what our biological systems use). D Form= meth (what we manufacture) |
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Molecules can be ______ & _______ apart |
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hydroxyl; polar; can hydrogen bond; hydrophillic |
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variable side chain that gives the unique physical and chemical properties of each amino acid-either nonpolar+hydrophobic or polar+charged (acidic/basic) |
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1. Hydroxyl 2. Aldehyde 3. Keto (carbon double bonded to an oxygen) 4. Carboxyl 5. Amino 6. Phosphate (1 phosphate & 4 oxygens will be negatively charged) 7. Sulfhydryl |
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molecules with the same atoms but a different layout |
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4 Main Classes of Macromolecules |
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1. Proteins 2. Carbohydrates 3. Lipids 4. Nucleic Acids |
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