OChem Chapter 12,14 Test – Flashcards
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Unlock answers| Fibrous Functions |
| structure and contractive |
| Fibrous Structure |
key: hiedrical structure
mostly non-polar amino acids are coiled together into super structures |
| Globular Functions |
Metabolic Work: -Catalysis -Transport -Regulation -Protection |
| Globular Structure |
| Soluble (hydrophilic side chains) |
| Fibrous Solubility |
| insoluble in water |
| Fibrous Structure (Primary…) |
|
| α-Keratines (where?) |
hair, skin, nails, horns, hoofs, wool (Fibrous Proteins) |
| Strength of Fibrous Proteins |
| h-bonding and disulfide bridges between peptide chains |
| Hemoglobin Structure |
4 polypeptide chains (2-α and 2-β)
alpha-helices separated by beta-turns |
| Hemoglobin (where?) |
| blood |
| Myoglobin Structure |
| Only 1 polypeptide chain |
| Protein function ulitmately depends on… |
| primary structure (amino acid sequence) |
| Genetic Mutation |
| An alteration in the DNA structure of a gene that may in turn produce a change in the primary structure of a protein |
| Sickle-cell Hemoglobin |
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)) |
| Sickle-cell Anemia (where?) |
Western Africa likely because of high incidence of malaria |
| Denaturation |
| Loss of native conformation brought about by a change in envirnmental conditions, resulting in a loss of physiological function |
| Denaturation alters which structures |
| Alters secondary, tertiary and quaternary structures |
| Digestion |
Breaks peptide bonds and alters primary structure
Not denaturation |
| Denaturation (Globular vs. Fibrous) |
| Globular protein have weaker secondary forces and thus are denatured easier. |
| 7 Methods of Denaturation |
|
| Increased Temp |
Increased motion disrupts non-covalent attractions
Example: cooking and sterilization |
| UV and Ionizing Raditions |
Causes chemical reactions
Example: X-ray |
| Mechanical Energy |
| Example: Whipping Eggs |
| Changes in pH |
| Affects salt bridges |
| Organic Chemicals |
Affects hydrophoic interactions
Example: Rubbing Alcohol |
| Salts of Heavy Metals |
"Pb2+, Hg2+ and Ag+ react with sulfdryl groups and forms metal disulfide bridges
Example: Mecury Poisioning" |
| Oxidizing and Reducing Agents |
Oxidizing: forming disulfide bridges Reducing: breaking disulfide bridges
Example: Perm |
| Matabolism Functions |
|
| Catabolism |
Biochemical degradation/break-down of energy-containing compounds (energy releasing)
Exampe: Combustion of C6H12O6, opposite of photosynthesis |
| Catabolism Process |
Nutrient molecules ↓ Precursor Molecules ↓ Acetyl CoA ↓ Water and Carbon Dioxide |
| ATP |
adenine triphosphate
Used for energy required processes |
| NADH |
nicotinamide adenine…
Used to make ATP |
| Stages 2 & 3 |
| use much of energy to create energy carrier molecules (ATP and NADH) |
Catabolism (oxidation or reduation) |
Oxidation process
low energy → high energy |
Anabolism (oxidation or reduation) |
Reduction process
high energy → low energy |
| Enzymes |
|
| Active Site |
|
| Anchor Points |
|
| Substrate |
| Reactant molecule |
| Complementarity |
| Enzymes highly specific to their substrates |
| Induced Fit |
| Protein/enzyme changes space as the substrate binds |
| Lock and Key |
| Enzyme doesn't change shape, fits directly into active site |
| True Substrate |
| the reactant that in supposed to react |
| Substrate Analog |
| a molecule similar to the true substrate (size, shape, charge, polority) |
| Competitive Inhibitor |
| Substrate analog that binds in the active site (binds but doesn;t react) |
| Non-competitive Inhibitor |
| ;alosteric;-a molecule that binds to a region other than the active site causing the conformation change which prevents the true substrate from binding |
| Cofactors/Coenzymes |
| ions/molecules that are needed to complete a protein's structure so that in can function |
| Apoenzyme |
| (apoprotein) polypeptide portion |
| Haloenzyme |
Entire functional protein/enzyme
Cofactors/coenzymes + apoenzyme = haloenzyme |
| Riboflavin |
| in FAD |
| Niacin |
| in MAD |
| Covalent Modification |
| enzyme activity is regulated by covalently attaching a group which either activates or deactivates that enzyme's activity |
| Feedback Inhibition |
| when the product of one reaction serves as an inhibitor for a previous reaction |
| Regulatory Enzymes |
| enzymatic activity controlled by binding of activators/inhibitors |
