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X-Phar410
Protein Structure and Function
| Question | Answer |
|---|---|
| causes premature fusion of infant skull bones | Muenke syndrome |
| Mutation of Glu6 to Val in hemoglobin; causes cell to sickle | sickle cell anemia; malaria resistance |
| Gly12 --> Val; Ras enzyme continuously active | cancer; "Ras" always turned on; unregulated cell growth |
| primary; secondary; tertiary; quaternary | order of structures |
| segments of a ploypeptide chain; 3-D arrangement; alpha helix and beta sheets | secondary structures |
| polypeptide segments without distinctly folded arrangement | random coil |
| 2 amino acids that interfere with alpha helix | Glycine and Proline |
| Parallel | --> --> --> |
| antiparallel | --> <-- --> |
| compact, highly-folded proteins that are water-soluble | GLOBULAR PROTEINS |
| stiff, elongated proteins that tend to form insoluble fibers | Fibrous Proteins |
| the 3-dimensional arrangement of multiple, folded peptide chains to form a single functioning protein | quaternary structure |
| Proteins that have only one polypeptide chain have no quaternary structure. | no answer |
| hemoglobin is what structure | quaternary |
| arrangements of secondary structural elements; "motifs" or "domains" | Supersecondary structures; usually not complete proteins themselves, but are protein COMPONENTS that have SPECIFIC functions |
| “Helix-turn-helix” motif that contains residues for binding Ca2+ | EF- hand domain |
| two antiparallel beta strands and an alpha helix, all held together by a bound zinc cation; bind DNA | Zinc fingers |
| A normal brain prion consists mostly of | a-helices and random coil |
| Disease causing prions aggregate to form insoluble amyliod fibers; extensive Beta sheet structures | no answer |
| Both diseased and normal prions have the same amino acid sequence, but the diseased prion is | stiff, tends to aggregate, limited resistance to digestion by proteases |
| diseased prion does not propagate by viral, bacteria, or other genetic means; what happens? | normal prions REFOLD into diseased shape (tertiary shape change) |
| Examples of prion disease | Creutzfeldt-Jakob disease(humans); Bovine Spongiform Encephalopathy (“mad cow” disease;Scrapie (sheep);Chronic Wasting Disease (elk/deer) |
| fibrous protein found in cartilage, tendons, bones, blood vessel walls, the lens of the eye, and skin | Collagen; 3 collagen strands support cell- triple helix called tropocollagen |
| required to maintain collagen’s quaternary structure | Hydroxylation of lysine(lysyl hydroxylase) and proline(prolyl hydroxylase) residues, generating hydroxylysine and hydroxyproline;both enzymes use vitamin C as a cofactor |
| fibrous protein found in cartilage, tendons, bones, blood vessel walls, the lens of the eye, and skin | Collagen; 3 collagen strands support cell- triple helix called tropocollagen |
| required to maintain collagen’s quaternary structure | Hydroxylation of lysine(lysyl hydroxylase) and proline(prolyl hydroxylase) residues, generating hydroxylysine and hydroxyproline;both enzymes use vitamin C as a cofactor |
| Prolonged vitamin C deficiency leads to | loss of collagen quaternary structure, bleeding gums, loose teeth, skin lesions, weakened blood vessel walls (bruising), and poor wound healing. These are all manifestations of SCURVY |
| group of disorders of the skin, joints, and connective tissues that can result in symptoms such as hyperelastic, thin skin, tissue fragility and bruising, poor wound healing, and hyperflexible joints | Ehlers-Danlos syndrome |
| (type VI);caused by genetic mutations that reduce or completely eliminate lysyl hydroxylase activity,;results in compromised collagen quaternary structure. | Ehlers-Danlos syndrome (type VI) |
| Proteins can be denatured by | heat; mechanical agitation; pH; detergents; organic solvents;chaotropic agents (urea or guanidinium) |
| an egg white thats heated is an example of | denatured albumin |
| Hb | Hemoglobin |
| Mb | Myoglobin |
| increases effective O2 solubility | Hemoglobin |
| found in muscle cells, for O2 storage | myoglobin; globular protein of 153 amino acids |
| found in red blood cells, for O2 transport | hemoglobin; quaternary structure |
| prosthetic group; ex: heme | a non- protein component that is permanently attached to a protein and is required for protein function |
| Heme is attached permanently but not covalently to | myoglobin and hemoglobin |
| the polypeptide part of an conjugated protein | Apoprotein |
| the complete, biologically active protein conjugate, consisting of the folded polypeptide chain(s) and any relevant prosthetic groups or cofactors | Holoprotein |
| Protein folding (tertiary structure) is driven primarily by | The hydrophobic effect and Electrostatics (dipoles, H-bonding, ion pairing/salt bridges) |
| percent of blood volume occupied by red blood cells | hematocrit; normal levels are 38-53% |
| a condition resulting from a deficiency of functional RBC's and/ or hemoglobin | anemia |
| A heterocyclic aromatic compound | porphyrin; Hemoglobin is porphyrin with Fe2+ |
| Stabilizes HbO2 | Histidine |
| Sublethal exposure to CO can cause | headache, confusion, fainting, and permanent damage to oxygen-sensitive tissues like the brain |
| Symptoms of CO poisoning begin at | 7% saturation of hemoglobin, and death can occur above 25% saturation. Smokers maintain a steady-state of about 4-8% hemoglobin saturation. |
| refers to proteins that can adopt alternate conformations/shapes | allostery |
| compounds that bind at sites other than the active catalytic site and regulate the enzyme through conformational changes affecting the catalytic site are? | Allosteric activators or inhibitors |
| Tight T-conformation plus oxygen leads to what? | Relaxed R- conformation |
| In the lung capillaries, pO2 is | ~100 mm Hg. (12kPa); capillaries of extrapulmonary tissues,range is 20-40 mm Hg (4kPa). |
| Myoglobin is half-saturated with O2 at pO2 = | 1-4 mm Hg |
| Hemoglobin is half-saturated with O2 at pO2 = | 26 mm Hg |
| Even after releasing O2 to the tissues, total Hb remains | 60-70% oxygenated; sufficient to maintain life for several minutes following acute respiratory arrest |
| Helps Body Adapt to Low pO2 | 2,3-BPG (2,3-bisphosphoglycerate); potent modifier of hemoglobin binding affinity |
| The BPG concentration in normal human blood is about | 5 mM at sea level and about 8 mM at high altitudes; hemoglobin binds to oxygen tightly when BPG is absent |
| HbF | Fetal Hb; y chains instead of b chains; fewer residues in y chains for binding 2,3-BPG; leads to looser binding and less stabilization of the HbF T-conformation by 2,3-BPG and therefore greater HbF affinity for O2 at reduced O2 concentrations. |
| HbA | Adult Hb |
| As the pH decreases, so does the affinity of Hb for O2 | Bohr effect |
| hemoglobin carries two end products of cellular respiration | transports H+(40%) and CO2(20%) |
| the affinity of hemoglobin for oxygen decreases as H+ and CO2 are bound and O2 is released to the tissues | At the relatively low pH and high CO2 concentration of peripheral tissues; it drops off oxygen and takes back H+ and CO2;opposite happens in lungs |
| a metabolic product of tissues with low O2 levels; can also Lower pH. | lactic acid |
| A consequence of the Bohr Effect is that O2 is preferentially released in areas of high metabolism that have a low pO2. | no answer |
| transports CO2 away from tissues and back to the lungs to be exhaled | Carbamino hemoglobin |
| promotes O2 release by lowering the pH; also lowers O2 affinity when it becomes non-enzymatically bound to the amino terminus of a Hb subunit | CO2 |
| CO2 is more soluble in plasma than O2 | true; can also be converted in blood to HCO3-, which is very soluble (filtered by kidneys) |
| The Protein Players (60-95% of total muscle protein): | Actin, Tropomyosin, Troponin, Myosin |
| Two of these coil to make the thin filament core | actin fibers |
| fibrous protein containing two a-helices coiled around each other; muscle | Tropomyosin |
| trimeric globular protein complex that binds the tropomyosin strands at regular intervals; binds Ca2+. | Troponin |
| contains two ~200 kDa heavy chains and four ~20 kDa light chains. | myosin; heavy chains have intertwining a-helical tails and globular heads |
| myosin bundles into hundreds of proteins to from | thick filaments |
| thin filaments | actin |
| vertical M disks connect | the horizontal thick myosin |
| vertical Z disks connect | the horizontal thin actin |
| the space between Z- disks | sarcomere; single contractile muscle unit |
| regions where no myosin; only actin in this light area | I band |
| region of myosin; actin overlap; dark | A band |
| Ca++ concentration increases to trigger muscle contraction | no answer |
| is the major class of antibody molecule and one of the most abundant proteins in the blood serum | immunoglobin G (IgG) |
| splits the heavy chains in the hinge region of the IgG molecule | Papain |
| splits the heavy chains beyond the disulfide bonds that join them at the hinge region | Pepsin |
| antibodies produced by many different B lymphocytes responding to one antigen (protein), such as a protein injected into an animal. | polyclonal antibodies; mix of antibodies that detect different parts of an antigen |
| synthesized by a population of identical B cells (a clone) grown in cell culture. These antibodies are homogeneous, all recognizing the same epitope | monoclonal antibodies |
Created by:
angieryx
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