under certain conditions alpha helical bundles can form and can facilitate protein insertion into membranes. discuss how they coudl achieve this at a biochemical level
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under certain conditions alpha helical bundles can form and can facilitate protein insertion into membranes. discuss how they coudl achieve this at a biochemical level?
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- Cone snails are carnivores that inject a powerful set of toxins into their prey, leading to rapid paralysis. Many of these toxins are found to bind to specific ionchannel proteins. Why are such molecules so toxic? How might such toxins be useful for biochemical studies?Will rate ASAP Which of the following amino acid residues would not provide a side chain for acid-base catalysis at physiological pH? (Assume pK values of each amino acid are equal to the pK value for the free amino acid in solution.) I. leucine II. lysine III. aspartic acid IV. histidine A) I, II, III B) I, II C) I D) II E) I, IIITheoretical and experimental measurements show that in many cases, thecontributions of ionic and hydrogen-bonding interactions to ΔH for proteinfolding are close to zero. Provide an explanation for this result.
- Determine whether a protein can act the same way in two different types of cells and whether it is conceivable for the same protein even if its basic mechanism is constant, to function in separate biochemical pathways in eye cells and muscle cells.Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a side chain for acid-base catalysis at physiological pH (assume pK of each amino acid is equal to pK value for the free amino acid in solution). Explain for each amino acid how and why each would or would not provide the side chain residue to support acid-base catalysis at physiological pH.affinity of a protein-protein or protein-ligand interaction can be described by the Dissociation Constant, Kd (written below). Consider a protein P and its inhibitor, I. I inhibits P's activity when bound to it: koff _ [A][B] Dissociation Constant: Ka = koN [AB] Question When [I] is 10-7 M, 99% of P's activity is inhibited. What is the Kd of this Protein- Inhibitor interaction?
- Protein concentration can readily be determined using the Beer-Lambert law: A = e l c where A = absorbance e = molar absorption coefficient (M-1cm-1) l = light path length (cm) c = concentration (M) If the molar absorption coefficient at 280 nm for yeast ADH is 48860 M-1cm-1 and a 10 mL solution of the protein has an absorbance at 280 nm of 0.4 (as measured by a spectrometer with pathlength 1 cm), then what is the concentration of the protein solution (in μM)? i.e. concentration = ______ μM If the molecular weight of the protein is 36849, what is its concentration in mg/mL? i.e. concentration = _______ mg/mL For each part of the question, show your calculations to arrive at your answers.Nonspecific elution of affinity bonded macromolecules is used in affinity chromatography explain why?Provide examples of biochemical phenomena that are directly affected by macromolecular crowding.
- Give the general Adiar equation for the binding of a ligand to a dimeric protein. Explain further what your understanding is of the terms "no-, positive-, and negative cooperativity” and graphically present the relationship between Ȳ and [S] for each of these cases. Also, give the relationship between the constants Kb1 and Kb2 in each case.An engineered ligand binds its target with 5 nM affinity at high pH. However, protonation of a histidine residue in the binding site of the ligand renders it unable to bind. Plot the ligand:target complex concentration versus the initial ligand concentration (in protonated or unprotonated form) at pH 4, 5, 6, 7, or 8 (five lines on one plot). Use a total target concentration of 10 nM.Calculate the concentration of the ligand required to fill 25% of the binding site. X+A ⇌ XA , ka = 1.5 ×10-6 Y+A ⇌ YA , ka = 4.7 × 10-4 (i.e, q = 0.25) for both proteins.