Term
| The 6 functions of the protein |
|
Definition
| Structural, regulatory, contractile, immunological, transport, and catalytic |
|
|
Term
| Form structural framework |
|
Definition
| Structural protein function |
|
|
Term
| alters cell function (hormones, neurotransmitters, receptors) |
|
Definition
|
|
Term
| Allows shortening of muscle cells |
|
Definition
|
|
Term
| aid responses that protect body again foreign substances and invading pathogens |
|
Definition
|
|
Term
| carry vital substances throughout body |
|
Definition
|
|
Term
| enzymes that regulate biochemical reactions |
|
Definition
|
|
Term
| ______ interact with other molecules (ligands) to carry out its function |
|
Definition
|
|
Term
| _____ must fit precisely into binding site |
|
Definition
|
|
Term
| many bonds between the ligand and the side chains of the proteins in binding site need to be formed to ______ |
|
Definition
|
|
Term
| individual bonds are ____ |
|
Definition
|
|
Term
| gives a protein its unique function |
|
Definition
|
|
Term
| determines types and location of binding sites |
|
Definition
|
|
Term
| Types of bonds holding ligand |
|
Definition
| Non-covalent bonds (H bonds, ionic bonds, van der waals attraction, hydrophobic interactions) |
|
|
Term
| If change conformational shape of protein then.... |
|
Definition
| the characteristics of binding site may change |
|
|
Term
| If the characteristics of the binding site change then the.... |
|
Definition
| ligand will not fit in site or not enough bonds will be made to hold ligand in place. |
|
|
Term
| denaturation causes change of conformational shape due to ______ |
|
Definition
|
|
Term
| Altered environment could be cause of the following: |
|
Definition
| Temperature, pH, or electrolyte concentration change |
|
|
Term
| denaturation disrupts the _____ bonds maintaining secondary, tertiary, and quaternary structure |
|
Definition
|
|
Term
| all proteins have a _____ lifetime within the cell |
|
Definition
|
|
Term
| Proteins are degraded because of: (list) |
|
Definition
| Normal turnover or renewal, mechanism of cellular control, cellular adaptation, damaged, misfolded |
|
|
Term
| Mechanism of cellular control: give the i.e. |
|
Definition
|
|
Term
| Cellular adaptions: give the i.e. |
|
Definition
| muscle atrophy when stop exercising |
|
|
Term
| short lived vs. long lived proteins is an example of: |
|
Definition
| normal turnover or renewel |
|
|
Term
| in the ubiquitin-proteasome system the protein is tagged with ____ |
|
Definition
|
|
Term
| recognize specific degradation signals on proteins, then adds a chain of ubiquitin |
|
Definition
|
|
Term
| recognizes tag and degrades the protein |
|
Definition
|
|
Term
|
Definition
| 20s cylinder and 19s caps (2) |
|
|
Term
|
Definition
|
|
Term
| recognizes ubiquittin on the protein as tag for destruction and unfolds protein and feeds it into the chamber |
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| catalysts _____ the activation energy |
|
Definition
|
|
Term
| lowers the activation energy means: |
|
Definition
| the amount of energy required for a reaction to take place |
|
|
Term
| to convert the substrate into a ____ state is based on the amount of energy required for a reaction to take place. |
|
Definition
|
|
Term
| catalyst convert substrate into product by: |
|
Definition
| making or breaking covalent bonds |
|
|
Term
| catalysts ______ up the rate of a reaction that would normally be too slow |
|
Definition
|
|
Term
| Catalyst increases rate by ______ |
|
Definition
|
|
Term
| enzymes have at least ____ binding sites |
|
Definition
|
|
Term
| is where the substrate bind |
|
Definition
|
|
Term
| where other molecules can bind to allosterically regulate the activity of the catalytic site |
|
Definition
|
|
Term
| The two binding sites for enzymes |
|
Definition
| Catalytic site and Regulatory site |
|
|
Term
| hydrolytic cleavage reaction |
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| synthesize molecules in anabolic reaction |
|
Definition
|
|
Term
| rearrange bonds within a single molecule |
|
Definition
|
|
Term
|
Definition
|
|
Term
| add phosphate groups to molecules |
|
Definition
|
|
Term
| remove phosphate groups from molecules |
|
Definition
|
|
Term
| catalyze reactions in which one molecule is oxidized and the other reduced |
|
Definition
|
|
Term
|
Definition
|
|
Term
| catalyzes condensation reactions in which two atoms are joined using ATP or GTP |
|
Definition
|
|
Term
| remove pairs of hydrogen atoms |
|
Definition
|
|
Term
| small molecule that functions as a transient carrier of a functional group |
|
Definition
|
|
Term
| Pyruvate + NADH+ H(+) ---> Lactate + NAD(+) is an example of... |
|
Definition
|
|
Term
| inorganic ion or molecule that is required for enzyme activity |
|
Definition
|
|
Term
| cytochrome oxidase required Fe(+2), Cu(+2) is an example of .... |
|
Definition
|
|
Term
| glutathione peroxidase requires Se is an example of |
|
Definition
|
|
Term
| One the proteasome is degraded, liberated amino acids can be used for: |
|
Definition
| gluconeogenesis or protein synthesis |
|
|
Term
| when a catalyst lowers the activation energy it: |
|
Definition
| brings substrates in close proximity, and holds substrate in a conformation that makes it easier to convert to product |
|
|
