Are all the proteins separated properly using two-dimensional (2D) gel electrophoresis? Why or why not?
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A: Thanks a lot for submitting question, you can find solution for both questions below.
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Are all the proteins separated properly using two-dimensional (2D) gel electrophoresis? Why or why not?
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- 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.…Spinal fluid contains 15 to 45 mg/dL protein. If you were to take a 5.0 mL sample of spinal fluid, how much protein could you expect to find? Express your answer as a range.Given that the normal range for serum protein is about 7 g/100ml and albumin is about 4 g/100ml, what clinical conclusions can you draw from the following samples A-C? If samples are not normal, what protein fraction is increased/decreased and with what disease is this protein pattern likely to be associated? Sample A: total protein = 14 g/100mlalbumin= 8 g/100 ml Sample B:total protein = 5.8 g/100ml albumin = 4 g/100 ml Sample C:total protein = 3.5 g/100mlalbumin = 2g/100 ml
- How many hemoglobin molecules are there in an average red cell? Assume that the molecular weight of the human hemoglobin tetramer is 65 kDa.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. Based on this information alone, what does the sickle-cell hemoglobin exhibit? A) only altered primary structure B) only altered tertiary structure C) only altered quaternary structure D) altered primary structure and altered quaternary structure; the secondary and tertiary structures may or may not be alteredThe interactions between the 2 a and 2 b subunits of hemoglobin represent what type of protein structure?
- Given the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3. (IF YOU COPY UR ANSWER FROM ANOTHER WEBSITE I WILL DISLIKE)Give 2 structural features in each of the given proteins below that make them perform their biological roles effectively (structural features that directly make them effective in their respective biological roles). Explain how each structural feature directly contributes to proteins’ biological roles. hemoglobin immunoglobulinCreatinine, C4H7N3O, is a by-product of muscle metabolism, and creatinine levels in the body are known to be a fairly reliable indicator of kidney function. The normal level of creatinine in the blood for adults is approximately 1.0 mg per deciliter (dL) of blood. If the density of blood is 1.025 g/mL, calculate the molarity of a normal creatinine level in a 10.0 mL blood sample.
- Describe the effect of the amino acid change on protein function: how does the HbS protein function differently than the HbA protein in red blood cells?If a commercially available insulin preparation contains 1 ppm of proinsulin, how many micrograms of proinsulin would be contained in a 10-mL vial of insulin?What is the molecular weight of the Botulinum neurotoxin, a protein that contains 1350 amino acids? Assume an average distribution of amino acids
