Term
|
Definition
| structure and contractive |
|
|
Term
|
Definition
key: hiedrical structure mostly non-polar amino acids are coiled together into super structures |
|
|
Term
|
Definition
Metabolic Work: -Catalysis -Transport -Regulation -Protection |
|
|
Term
|
Definition
| Soluble (hydrophilic side chains) |
|
|
Term
|
Definition
|
|
Term
| Fibrous Structure (Primary…) |
|
Definition
- No tertiary
- Usually have quaternary
|
|
|
Term
|
Definition
hair, skin, nails, horns, hoofs, wool (Fibrous Proteins) |
|
|
Term
| Strength of Fibrous Proteins |
|
Definition
| h-bonding and disulfide bridges between peptide chains |
|
|
Term
|
Definition
4 polypeptide chains (2-α and 2-β) alpha-helices separated by beta-turns |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
| Protein function ulitmately depends on… |
|
Definition
| primary structure (amino acid sequence) |
|
|
Term
|
Definition
| An alteration in the DNA structure of a gene that may in turn produce a change in the primary structure of a protein |
|
|
Term
|
Definition
Region critical to binding oxygen are NOT changed Sickling is the aggregation of the hemoglobins (hydrophobic attractions between the hydrophobic pocket and residue 6 (Val)) |
|
|
Term
| Sickle-cell Anemia (where?) |
|
Definition
Western Africa likely because of high incidence of malaria |
|
|
Term
|
Definition
| Loss of native conformation brought about by a change in envirnmental conditions, resulting in a loss of physiological function |
|
|
Term
| Denaturation alters which structures |
|
Definition
| Alters secondary, tertiary and quaternary structures |
|
|
Term
|
Definition
Breaks peptide bonds and alters primary structure Not denaturation |
|
|
Term
| Denaturation (Globular vs. Fibrous) |
|
Definition
| Globular protein have weaker secondary forces and thus are denatured easier. |
|
|
Term
| 7 Methods of Denaturation |
|
Definition
- Increase Temp
- UV and ionizing Radiations
- Mechanical Energy
- Changes in pH
- Organic Chemicals
- Salts of Heavy Metals
- Oxidizing and Reducing Agents
|
|
|
Term
|
Definition
Increased motion disrupts non-covalent attractions Example: cooking and sterilization |
|
|
Term
| UV and Ionizing Raditions |
|
Definition
Causes chemical reactions Example: X-ray |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
Affects hydrophoic interactions Example: Rubbing Alcohol |
|
|
Term
|
Definition
"Pb2+, Hg2+ and Ag+ react with sulfdryl groups and forms metal disulfide bridges Example: Mecury Poisioning" |
|
|
Term
| Oxidizing and Reducing Agents |
|
Definition
Oxidizing: forming disulfide bridges Reducing: breaking disulfide bridges Example: Perm |
|
|
Term
|
Definition
Obtain energy in chemical form by degradation of nutrients Convert a wide vareity of molecules into a few precursor molecules Synthesize cell molecules Produce or modify biomolecules necessary for specific functions in specialized cells
|
|
|
Term
|
Definition
Biochemical degradation/break-down of energy-containing compounds (energy releasing) Exampe: Combustion of C6H12O6, opposite of photosynthesis |
|
|
Term
|
Definition
Nutrient molecules ↓ Precursor Molecules ↓ Acetyl CoA ↓ Water and Carbon Dioxide |
|
|
Term
|
Definition
adenine triphosphate Used for energy required processes |
|
|
Term
|
Definition
nicotinamide adenine… Used to make ATP |
|
|
Term
|
Definition
| use much of energy to create energy carrier molecules (ATP and NADH) |
|
|
Term
Catabolism (oxidation or reduation) |
|
Definition
Oxidation process low energy → high energy |
|
|
Term
Anabolism (oxidation or reduation) |
|
Definition
Reduction process high energy → low energy |
|
|
Term
|
Definition
- Organic Catalyst
- Can be denatured
- Proteins
|
|
|
Term
|
Definition
- Where the substrate binds
- Has anchor points
|
|
|
Term
|
Definition
- Hold the substrate in place
- Use IMF to do so
|
|
|
Term
|
Definition
|
|
Term
|
Definition
| Enzymes highly specific to their substrates |
|
|
Term
|
Definition
| Protein/enzyme changes space as the substrate binds |
|
|
Term
|
Definition
| Enzyme doesn't change shape, fits directly into active site |
|
|
Term
|
Definition
| the reactant that in supposed to react |
|
|
Term
|
Definition
| a molecule similar to the true substrate (size, shape, charge, polority) |
|
|
Term
|
Definition
| Substrate analog that binds in the active site (binds but doesn’t react) |
|
|
Term
| Non-competitive Inhibitor |
|
Definition
| "alosteric"-a molecule that binds to a region other than the active site causing the conformation change which prevents the true substrate from binding |
|
|
Term
|
Definition
| ions/molecules that are needed to complete a protein's structure so that in can function |
|
|
Term
|
Definition
| (apoprotein) polypeptide portion |
|
|
Term
|
Definition
Entire functional protein/enzyme Cofactors/coenzymes + apoenzyme = haloenzyme |
|
|
Term
|
Definition
|
|
Term
|
Definition
|
|
Term
|
Definition
| enzyme activity is regulated by covalently attaching a group which either activates or deactivates that enzyme's activity |
|
|
Term
|
Definition
| when the product of one reaction serves as an inhibitor for a previous reaction |
|
|
Term
|
Definition
| enzymatic activity controlled by binding of activators/inhibitors |
|
|
