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Physiology Ch. 2
Atoms/Ions
| Term | Definition |
|---|---|
| HCO3 - | Bicarbonate |
| PO4 3- | Phosphate |
| CO3 - | Carbonate |
| SO4 2- | Sulfate |
| NO3 - | Nitrate |
| Ionic bonds | Metal + nonmetal. Dissociates in water, lattice as solid, bound by electromagnetic forces |
| Molecular formula | Indicated # and type of atoms |
| Structural formula | Indicates #, type, and arrangement of atoms (OCO). Allows differentiation of isomers |
| Covalent bonds | Nonmetal + nonmetal |
| Electronegativity | Relative attraction of electron by atom |
| Polar covalent bond | From dissimilar covalent bond; unequal sharing. WATER |
| Nonpolar covalent bond | When 2 molec's electronegativity are similar. |
| Amphipathic molecules | Have region of polar and region of nonpolar |
| Hydrogen bonding | Occurs in proteins to fold them and DNA. |
| Free radicals | Molecules with unpaired electrons in outermost orbital. Are unstable and highly reactive, and cause damage to their surroundings. |
| Hydrolysis | Breaking down of molecules using H2O |
| Dehydration synthesis | Molecules are assembled by removing H2O |
| Osmosis | low solute conc. to high. Simple movement of H2O |
| H2O is the ______ solvent. | Universal. Surrounds substances in hydration shell |
| Hydrophilic | "water loving" |
| Hydrophobic | "water fearing" Fats and cholesteral |
| Hydrophobic exclusion | H2O molecules force out nonpolar molecules |
| Hydrophobic interaction | Excluded molecules |
| Acid | Proton donors ( HA -> H+ + anion) |
| Base | Proton acceptors (B- + H+ -> HB) |
| Buffers | Help precent pH change by accepting or donating H+ to neutralize acids/bases |
| Blood pH | 7.35 to 7.45 |
| Mixtures | Substances not chemically changed and able to be physically seperated |
| Suspension | Material greater than 1mm mixed with water. Appears cloudy |
| Colloid | Smaller molecules than suspension but larger than solution |
| Solution | Solute dissolved in solvent |
| Molarity | mol/L |
| Molality | mol (soln)/kg (solv) |
| Osmoles | Measures number of particles in solution |
| Osmolarity | # particles/Lsoln |
| Osmolality | # particles/kg H2O |
| Osmolality of blood | 300 m |
| Macromolecules | Carbohydrates, nucleic acids, lipids, proteins |
| Anabolism | Dehydration synthesis, small -> large molecules |
| Catabolism | Hydrolysis, large -> small molecules |
| Lipids | Contain C, H, and O. Nonpolar. Triglycerides, phospholipids, steroids, eicosanoids |
| Unsaturated | Contains double bond(s) |
| Saturated | All single bonds (Every C has enough H) |
| Triglycerides | 3 fatty acids + glycerol. Type of lipid |
| Phospholipids | Amphipathic, same as triglycerides but one side of glycerol has polar phosphate group |
| Steriods | Type of lipid that is hydrophobic. 4 carbon rings, includes cholesterol |
| Eicosanoids | Family of molecules made from fatty acid arachidonic acid (AA), present in phospholipids. |
| Most animal fats are ______ | Saturated |
| Most vegetable fats are ______ | Unsaturated |
| Carbohydrates | (CH2O)n |
| Monosaccharides | Glucose, cructose, galactose, ribose, deoxyribose |
| Disaccharides | Formed by 2 monosaccharides. Sucrose and lactose |
| Polysaccharides | Many monosaccharides. Glycogen, starch, cellulose |
| Glucose | 6C carbohydrate that is important for neurons for energy. Is what is measured when blood is taken. |
| Glycogen | Lots of glucose put together in liver |
| Nucleic acids | DNA and RNA, composed of nucleotides |
| Adenine Triphosphate | Releases energy when broken, is nucleotide |
| Purines | Double ring nitrogenous bases. A and G |
| Nucleotide | Monomer of nucleic acids made of sugar, phosphate group, and nitrogenous base |
| Pyrimidines | Single ring nitrogenous base (C, T, and U) |
| Proteins | C, H, O, N, and small amounts of other elements. Made of amino acids and humans need 20. Functions as catalysts, defense, transport, movement, support, regulation, and storage |
| Peptide bond | Bond type that links amino acids |
| Primary Structure | Protein structure determined by amino acid chain. Linear |
| Secondary Structure | Protein structure about the folding into alpha helix or beta pleated sheet |
| Tertiary Structure | Protein structure where hydrogen bonding allows protein to further fold |
| Quaternary Structure | Protein structure where multiple proteins interact |
| Denaturation | Affects 2, 3, and 4 structures of protein. Protein unravels, usually due to heat or pH change. |
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