In the binding of oxygen to myoglobin, the relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as: hyperbolic linear with a negative slope linear with a positive slope random sigmoidal
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- Suppose myoglobin is prepared with Zn²+ in the place of Fe²+ in the porphyrin. Would you expect this modified myoglobin to bind oxygen? No, because Zn²+ cannot partially transfer an electron to oxygen to form a complex. Fe²+ . Yes, because oxygen can form a bond with either Zn²+ 2+ No, because the larger size of Zn²+ will prevent the ion from fitting within the porphyrin ring. Yes, because oxygen binding to myoglobin depends solely on the presence of a distal histidine. orShortly after a person dies, Ca2+diffuses out of the saroplasmic reticulum and the body becomes very still and rigid, a phenomenoncalled rigor mortis (rig′er mōr′tis). Given ATP’s role in myosin head movement, propose an explanation for rigor mortis.Sickle-cell hemoglobin (HbS) differs from normal human adult hemoglobin (HbA) by a single mutational change, Glu6 S Val, which causes the HbS molecules to aggregate under proper conditions. Under certain conditions, the HbS filaments that form at body temperature disaggregate when the temperature is lowered to 0°C. Explain.
- It is not an easy matter to assign particular func-tions to specific components of the basal lamina, sincethe overall structure is a complicated composite materialwith both mechanical and signaling properties. Nidogen,for example, cross-links two central components of thebasal lamina by binding to the laminin γ-1 chain and totype IV collagen. Given such a key role, it was surprisingthat mice with a homozygous knockout of the gene fornidogen-1 were entirely healthy, with no abnormal phe-notype. Similarly, mice homozygous for a knockout of thegene for nidogen-2 also appeared completely normal. Bycontrast, mice that were homozygous for a defined muta-tion in the gene for laminin γ-1, which eliminated just thebinding site for nidogen, died at birth with severe defectsin lung and kidney formation. The mutant portion of thelaminin γ-1 chain is thought to have no other functionthan to bind nidogen, and does not affect laminin struc-ture or its ability to assemble into the basal lamina.…Explain how the overall three-dimensional shape of myoglobin allows it to function as an oxygen-storage moleculeThe primary and tertiary structures of hemoglobin and myoglobin are very similar and both contain the 'heme' group as an oxygen-binding prosthetic group. However this There are important functional differences between the two proteins. Hemoglobin oxygen transport protein, myoglobin functions as oxygen storage protein. Hemoglobin and consider the structural differences and oxygen binding curves between myoglobin why myoglobin is a good oxygen transport protein, while hemoglobin Explain why it cannot be a good oxygen storage protein.
- Calculate the percent oxygen saturation of myoglobin if 7 of 15 binding sites are occupied..Certain multi-headed myosins bind cooperatively to actin filaments. The binding interaction is mainly electrostatic in nature, so the presence of additional salt (ions) in solution can interfere with binding; ions will tend to associate with charged residues on the two proteins, blocking electrostatic attractions that would otherwise take place. Briefly describe the expected shape of the binding curve for one of these myosins, and what will happen to the shape when the salt concentration increases.A few hours after the death of an animal, the corpse will stiffen as a result of continued contraction of muscle tissue (this state is called rigor mortis). This phenomenon is the result of the loss of ATP production in muscle tissue. (a) Consult Figure 7.48 and describe, in terms of the six-step model of mus- de contraction, how a lack of ATP in sarcomeres would result in rigor mortis. (b) The Ca* transporter in sarcomeres that keeps the [Ca*)-10-7 M requires ATP to drive transport of Ca* ions across the membrane of the sarcoplasmic reticulum. How would a loss of this Ca* transport func- tion result in the initiation of rigor mortis? (c) Rigor mortis is maximal at - 12 hrs after death, and by 72 hrs is no longer observed. Propose an explanation for the disappearance of rigor mortis after 12 hrs.
- During the cross-bridge in muscle cells, myosin motors hydrolyzes ATP as a fuel to create a pulling force on actin fibers. Please describe1) the myosin motors undergo different steps of ATP hydrolysis2) the state of the ATP nucleotide affects the binding and position of the myosin motor with respect to the actin fiberThe sarcoplasmic reticulum Ca2+-ATPase, pumps 2 mol Ca2+ out of sarcomeres per mol ATP hydrolyzed. Part A: Given the following steady-state concentrations and a membrane potential of 64 mV (inside negative), calculate ΔG for the following active transport process at 37 ∘C and pH=7.4: 2Ca2+(in)+ATP+H2O→2Ca2+(out)+ADP+Pi+H+ ATP=2.8mM,ADP=206μM,Pi=5.4mM,Ca2+(in)=34μM,Ca2+(out)=2.2mM The answer to part A was -7.4 kJ/mol I need help with Part B: Part B: The activity of the Ca2+-ATPase is regulated reversibly under normal conditions to maintain homeostatic concentrations of Ca2+ inside the sarcomere. However, in a rare genetic disorder, irreversible activation of the Ca2+-ATPase can occur. Assuming 37 ∘C, pH=7.4, and the steady-state concentrations for ATP, ADP Pi, and Ca2+(out) given in part (a) calculate the minimum [Ca2+] inside a sarcomere that has irreversibly activated Ca2+-ATPase (i.e., the Ca2+-ATPase activity is always “on”).As mentioned in class, one additional major use of ATP in skeletal muscle (besides powering the myosin heads) is the recycling of calcium ions back into the sarcoplasmic reticulum after depolarization. The resting concentration of Ca++ in the muscle cell cytoplasm is about 50-100 nM, and the spike concentration after depolarization is about 10-20 μΜ. a) Consider a single sarcomere. What is the number of free calcium ions within the sarcomere at rest? What is the number of free calcium ions after depolarization? b) The major ion pump responsible for calcium ion recycling is SERCA (sarco/endoplasmic reticulum calcium ATPase). SERCA uses one molecule of ATP to pump two calcium ions, and the resting level can be restored in about 10-20 ms. How many molecules of ATP are used in a single sarcomere for pumping calcium in a single "twitch"? c) Assume that a single "twitch" is sufficient to drive one sarcomere from its fully extended length (about 2.5 µm) to its fully contracted length (about 1…