Term
| How macromolecules are broken apart |
|
Definition
Via hydrolysis (H2O split into OH- and H+).
Macromolecules ---> Micromolecules + H2O |
|
|
Term
| How macromolecules are formed |
|
Definition
Via dehydration (lose water).
Micromolecules + H2O ---> Macromolecules |
|
|
Term
|
Definition
| Low solubility in water and high solubility in nonpolar organic solvents. Hydrophobic, make great barriers separating aqueous environments. |
|
|
Term
|
Definition
| Fatty acids, triacylglycerols, phospholipids, glycolipids, steroids, terpenes. |
|
|
Term
|
Definition
Building blocks for most complex lipids. Long chains of carbons with carboxylic acid at one end. Usually even number of carbons. Max in humans is 24 carbons. Saturated (only single C-C bonds) or unsaturated (one or more C=C bonds). Oxidation of them gives large amounts of chemical energy.
[image] |
|
|
Term
|
Definition
Also called triglycerides or fats and oils. Three-carbon backbone called glycerol which is attached to three fatty acids. Store energy, provide thermal insulation and padding.
[image] |
|
|
Term
|
Definition
| Fat cells. Specialized cells whose cytoplasm contains almost nothing but triglycerides. |
|
|
Term
|
Definition
Built from glycerol backbone. Polar phosphate group replaces one of the fatty acids. Phosphate group on opposite side of glycerol from the fatty acids, making it polar at the phosphate end and nonpolar at the fatty acid end (amphipathic). In membranes (structural).
[image] |
|
|
Term
|
Definition
| Similar to phospholipids, but have one or more carbohydrates attached to the glycerol backone instead of the phosphate group. Also amphipathic. In membranes of myelinated cells. |
|
|
Term
|
Definition
Four-ringed structures. Include hormones, vitamin D and cholesterol. Important in membranes, regulating metabolic activities.
[image] |
|
|
Term
|
Definition
|
|
Term
|
Definition
| 20-carbon, fatty acid-like. Include prostaglandins, thromboxanes and leukotrienes. Released from cell membranes as local hormones (regulate blood pressure, body temp, smooth muscle contraction, etc.) |
|
|
Term
|
Definition
Transport lipids in the blood. Lipid core surrounded by phospholipids and apoproteins. Dissolves lipids in its hydrophobic core, then moves freely through the aqueous solution due to its hydrophilic shell.
Classified by density (greater ratio of lipid to protein, lower density) - chylomicrons, very low density lipoproteins (VLDL), low density lipoproteins (LDL), high density lipoproteins (HDL).
VLDL and LDL bad b/c more lipid than protein. HDL good b/c more proetin than lipid. |
|
|
Term
|
Definition
| From chain of amino acids linked together by peptide bonds. Also called polypeptides. |
|
|
Term
| Essential (as in amino acids) |
|
Definition
| Body doesn't make it by itself; need to ingest. |
|
|
Term
|
Definition
| Side chains attached to alpha-Carbon. Digested proteins reach cells as single amino acids. In solution, amino acids always carry one or more charges (position & charge depends on pH). |
|
|
Term
| Amino Acids w/ Nonpolar R Groups |
|
Definition
Glycine:
[image]
Alanine:
[image]
Valine:
[image]
Leucine:
[image]
Isoleucine:
[image]
Phenylalanine:
[image]
Tryptophan:
[image]
Methionine:
[image]
Proline:
[image] |
|
|
Term
| Amino Acids w/ Polar R Groups |
|
Definition
Serine:
[image]
Threonine:
[image]
Cysteine:
[image]
Tyrosine:
[image]
Asparagine:
[image]
Glutamine:
[image] |
|
|
Term
| Amino Acids w/ Acidic R Groups |
|
Definition
Aspartic Acid:
[image]
Glutamic Acid:
[image] |
|
|
Term
|
Definition
Lysine:
[image]
Arginine:
[image]
Histidine:
[image] |
|
|
Term
|
Definition
| Number and sequence of amino acids in polypeptide. All proteins have this, most have secondary. |
|
|
Term
|
Definition
Single chain twists. Reinforced by hydrogen bonds between carbonyl oxygen and hydrogen on amino.
[image] |
|
|
Term
|
Definition
Single chain lies alongside itself. Connecting segments of two strands can lie in same direction (parallel) or opposite (antiparallel). Reinforced by hydrogen bonds between carbonyl oxygen and hydrogen on amino.
[image] |
|
|
Term
|
Definition
Larger proteins (globular, fibrous/structural, etc.) can have this and quaternary. 3D shape formed when peptide chain curls and folds.
[image] |
|
|
Term
|
Definition
Two or more polypeptide chains binding together.
[image] |
|
|
Term
Forces to Make
Tertiary and Quaternary Structures |
|
Definition
1. covalent disulfide bonds between two cysteine amino acids on different parts of the chain
2. electrostatic (ionic) interactions mostly between acidic and basic side chains
3. hydrogen bonds
4. van der Waals forces
5. hydrophobic side chains pushed away from water (toward center of protein) |
|
|
