420166
| Question | Answer |
| Isotopes | Elements that contain additional neutrons |
| Compound | substance composed of 2 or more elements in a fixed ratio |
| Covalent Bonds | build stable molecules to form when two atoms share one or more pairs of valence electrons. |
| Ionic Bonds | which form when atoms with opposite electrical charges (ions) attract. |
| Hydrogen bonding | These bonds form between the partially negative O atoms and the partially positive H atoms of two water molecules. |
| What is an ion? | A charged atom or molecule |
| Van der Waal’s forces | Short range attractive force between temporarily charged regions of two atoms or molecules |
| Living systems have seven characteristics in common | 1.Composed of one or more cells 2.Complex and highly ordered 3.Can respond to stimuli 4.Grow,reproduce, transmit genes 5.Energy to accomplish work 6.Homeostasis 7.Evolution |
| Protein Functions | |
| Peptide bond | The type of bond that links amino acids together in proteins through a dehydration reaction. |
| Polypeptide | A molecule consisting of many joined amino acids; not usually as complex as a protein. |
| Hydrogen Bond |
Image:
Hydrogen_bond (image/jpg)
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| Covalent Bond |
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Disulfide_bridge (image/jpg)
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| Ionic Bond |
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Ionic_bond (image/jpg)
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| Van Der Waals attraction | |
| Hydrophobic | |
| Primary structure | The specific amino acid sequence of a protein. |
| Secondary structure | In a protein, hydrogen-bonding interactions between —CO and —NH groups of the primary structure. |
| Tertiary structure | The final folded shape of a globular protein |
| Quaternary structure | When two or more polypeptide chains associate to form a functional protein, the individual chains are referred to as subunits of the protein. The arrangment of these are called.. |
| The structure of proteins | |
| Chaperone proteins | A class of enzymes that help proteins fold |
| Denaturation | If a protein's environment is altered, the protein may change its shape or even unfold completely |
| Dissociation | reversible separation of protein subunits from a quaternary structure without altering their tertiary structure. |
| Cell theory | All organisms are composed of one or more cells, and the life processes of metabolism and heredity occur within these cells. Cells are the smallest living things, the basic units of organization of all organisms. Cells arise only by division of a previously existing cell. |
| Prokaryote | A bacterium; a cell lacking a membrane-bounded nucleus or membrane-bounded organelles. |
| Nucleoid | The area of a prokaryotic cell, usually near the center, that contains the genome in the form of DNA compacted with protein. |
| Nuclear envelope | The bounding structure of the eukaryotic nucleus. |
| Eukaryotic cells | are far more complex than prokaryotic cells |
| Electron Transport chain | Electron carriers located in the mitochondrial inner membrane |
| Cellular respiration | energy is harvest, the oxidation of organic componds to extract energy from chemical bonds |
| Oxidation | An atom or molecule that loses an electron |
| Aeroboic respiration | When the acceptor is oxygen |
| Anaerobic Respiration | when the acceptor is somthing other than oxygen |
| thermodynamics | the branch of chemistry concerned with energy change |
| the 1st law of thermodynamics | amount of energy in the universe, energy can't be created or destroyed, only changed form |
| the 2nd law of themodynamics | the transformation of potential energy into heat or random molecular motion during any energy translation disorder is increasing (Entropy) |
| Entropy | measure of randomness in a system, energy |
| Fermentation | Organic molecule as final electron acceptor |
| Glycolysis | Occurs in cytoplasm and converts glucose into 2 3-carbon molecules of pyruvate |
| Dehydrogenations | Electrons lost accompanied by protons hydrogen atom is lost |
| Multienzyme Complexes | often several enzymes catalizing different steps of a sequence of reactions are associated with one another in noncovalently bonded assemblies |
| Inhibitor | A substance that binds to an enzyme and decreases its activity |
| Competitive Inhibitors | An inhibitor that binds to the same active site as an enzymes substrate, competing with the substrate |
| phosphodiester bond | The linkage between two sugars in the backbone of a nucleic acid molecule; the phosphate group connects the pentose sugars through a pair of ester bonds. |
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