Explain, which site of the heme structure, A or B, is this prosthetic group plugged into the core moiety of the myoglobin globe? CH3- CH₂ CH₂ HC CH-C CH₂ C-N CH3 A B CH₂ CH₂ N=C CH C-CH3 CH C-CH3 CH₂
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- Theoretically, the pI of myoglobin is 7.2. In phosphate buffer pH 6.0, what is the overall charge of myoglobin? How would it interact with CM Sepharose?Hemoglobin has two alpha-type chains and two beta-type chains. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Myoglobin has much helix-turn-helix motif. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Myoglobin folds up into a ball-like structure. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure Domains differ from subunits in that: a) subunits are connected by peptide bonds while domains are not b) domains are connected by peptide bonds while subunits are not c) subunits are larger than domains d) subunits are hydrophobic while domains are hydrophilicOne molecule of 2,3-BPG binds to one tetramer of hemoglobin in a central cavity of the hemoglobin molecule. Is the interaction between BPG and hemoglobin stronger or weaker than it would be if BPG bound to the surface of the protein instead? Explain your answer (hint: think about how these different situations affect the dielectric constant). (Please provide clear and sufficient explanation for the question, thank you!)
- What is inositol trisphosphate (IP3)?If instead of using 3.5 µM myoglobin (receptor) you used half of this (that is, 1.75 µM myoglobin), what would be that value of the Kd, that you calculated ( how would it change)? Please explain so I can solve on my own :) (How does changing concentration of the receptor in a ligand-receptor binding experiment affect the dissociation constant?)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.
- using examples, discuss the classification of proteins into fibrous and globular classification. - I would want to use myoglobin as an example of glubular but I don't know if that falls in the category for fibroushow do salt bridges that include amino-terminal carbamate stabilize the deoxy form of hemoglobin. Please answer it asap.... With detailed explanation...From the figure of O2 binding to myoglobin and hemoglobin (ignore the linemarked as T) as described in lecture (shown below) answer the following questions. a) Estimate the P50 for myoglobin from the plot. Show how this estimation isdetermined from the binding curve above. ( The first ghraph) b)Using YO2 = PO2/P50 + PO2 , calculate the fraction of O2 bound for myoglobin at 1 torr. (2nd graph) c)Using the binding curve on the previous page, show how you can estimate whatfraction of hemoglobin is bound near tissues at a pO2 of 30 torr and provide this value. If the pH were lowered, will the amount of O2 bound to hemoglobin at 30 torr increaseor decrease? Explain why this is so based on how this changes hemoglobin structure. If 2,3-BPG were added to the solution, will the amount of O2 bound to hemoglobin at30 torr increase or decrease? Explain why this is so based on how this changes hemoglobinstructure.
- The molecular formula for glucose is C6H12O6. What would be the molecular formula for a polymer made by linking ten glucose molecules together by dehydration reactions? Group of answer choices A. C60H120O60 B. C60H102O51 C. C60H100O50 D. C60H111O51 Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)In sickle-cell disease, as a result of a single amino acid change, the mutant hemoglobin tetramers associate with each other and assemble into large fibers.…In a Myoglobin and azide ligand-receptor binding experiment, instead of using 3.5 µM myoglobin you used half of this (1.75 µM myoglobin), what would be that value of the Kd, that you calculated (how would the Kd change)?Magnesium blocks voltage-gated calcium channels on the membrane of smooth muscle cells. How do barium ions affect smooth muscle on the molecular level?