Sedimenting spheres. What is the dependence of the sedimentation coefficient s of a spherical protein on its mass? How much more rapidly does an 80 -kDa protein sediment than does a 40-kDa protein?
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Sedimenting spheres. What is the dependence of the sedimentation coefficient s of a spherical protein on its mass?
How much more rapidly does an 80 -kDa protein sediment
than does a 40-kDa protein?
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- Ionization State of Histidine.Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. 1.Histidine has three ionizable functional groups. Write the equilibrium equations for its three ion-izationsand assign the proper pKa for each ionization. Draw the structure of histidine in each ionization state.What is the net charge on the histidine molecule in each ionization state? 2.Which structure drawn in (1) corresponds to theionization state of histidine at pH 1, 4, 8, and12?Note that the ionization state can be approximated by treating each ionizable group independently. 3.What is the net charge of histidine at pH 1, 4, 8, and 12? For each pH, will histidine migrate to-ward the anode (+) or cathode (-) when placed in an electric field?Peptide mass determination. You have isolated a proteinfrom the bacterium E. coli and seek to confirm its identityby trypsin digestion and mass spectrometry. Determinationof the masses of several peptide fragments has enabled youto deduce the identity of the protein. However, there is adiscrepancy with one of the peptide fragments, whichyou believe should have the sequence MLNSFK and an(M 1 H)1 value of 739.38. In your experiments, yourepeat edly obtain an (M 1 H)1 value of 767.38. What isthe cause of this discrepancy and what does it tell youabout the region of the protein from which this peptide isderived?More ratios. Through the use of nuclear magnetic resonance spectroscopy, it is possible to determine the ratio between the protonated and deprotonated forms of buffers. (a) Suppose the ratio of [ A- ]A I to [HA] is determined to be 0.1 for a buffer with pKar6.0.pKa = 6.0. What is the pH? (b) For a different buffer, 91974 suppose the ratio of [ A- ]lA J to [HA] is determined to be 0.1 and the pHpH is 7.0. In this case, what is the pKapKa of the buffer? (c) For another buffer with pKa=7.5PKa = 7.5 at pH 8.0pH 8.0, what is the expected ratio of [ A- ][A ] to [HA]? do
- Shape and dimension. (a) Tropomyosin, a 70-kDa muscle protein, is a two-stranded α-helical coiled coil. Estimate the length of the molecule. (b) Suppose that a 40-residue segment of a protein folds into a two-stranded antiparallel β structure with a 4-residue hairpin turn. What is the longest dimension of this motif?2. Subunit Composition of a Protein. A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography ( F). When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (=), three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein. Note: dithiothreitol is a reagent to beak down the disulfide bonds.V-A. Which of the following amino acids will elute first in a cation-exchange column using a buffer at pH 7? 1. Asp or Lys 2. Arg or Met 3. Gly or Val 4. Ser or Ala
- Could you please help me with this question? I am struggling. Thanks in advance. Describe the four levels of protein structure: primary, secondary, tertiary, and quarternary.Choice and Preparation of a Buffer System1. Choosing the proper buffer solution In Protein Precipitation, two liters of 5mM buffer solution with pH 5.2 is needed in the isolation of albumin. Which among the following buffer solution is best fitted for said purpose? Justify your answer.Buffer solutions pKa Acetate buffer 4.73Tris- (hydroxymethy) aminomethane 8.08Phosphate buffer 7.20 2. Preparation of the chosen buffer system Calculate and measure the amounts (in grams if solid and in mL if liquid) of weak acid and conjugate base needed to be able to prepare the chosen buffer system in part A above. Express your answer in useful units (that is, prepare it from practical amounts or concentrations of starting materials).Purification of a new unknown protein that you isolated from tissue and Assume that you have reached the following data during the characterization; Gel filtration: Gel filtration in protein native conformation When chromatographed, it has a molecular weight of 240000 daltons (240 kDa) is detected to be around. Gel filtration: The same protein is first denatured with 6 M guanidinium hydrochloride subjected to gel filtration chromatography again under denatured conditions. is retained, and the only column from the column with a molecular weight of about 60000 daltons (60 kDa) a protein is obtained. SDS-PAGE: Protein finally SDS-PAGE in the presence of beta-mercaptoethanol (Sodium dodecyl-sulphate polyacrylamide gel electrophoresis) analysis being held. As a result of SDS-PAGE analysis, their weight in the gel is approximately 40000 daltons. Two protein bands corresponding to (40 kDa) and 20000 daltons (20 kDa) is observed. In the light of these findings, the quaternary/quaternary…
- Predict the number of bands and apparent mol. wt. of the following proteins on SDS gels. 1. A trimeric protein containing three chains, each with a molecular weight of 60,000 Da (60 kDa).7 Protein structure.Circle one of the three amino acid sequences that is most likely to form a stable a-helix? RASKTARQ DASKTAEQ KPGKPAGQ In one sentence (that can be accompanied by a small picture) explain why?Hello, please help me with my assignment. Can you answer ALL QUESTIONS EXCEPT QUESTIONS 1-31. Which of the following statements is accurate regarding these protein structures?a. Proteins in a quaternary structure consist of a simple polypeptide chain.b. Interactions between the R groups in amino acids form tertiary structure.c. Secondary structures are formed by multiple polypeptide chains.d. The two types of primary structure are α- helices and β- pleated sheets. 2. What type of bonds are formed between amino acids?a. Peptide bondb. Glycosidic linkagec. Hydrogen bondsd. Ester linkages 3. Which of the following is an example of protein denaturation?a. Amino acids fold into repeating patterns due to hydrogen bonding of the peptide backbone.b. Several amino acids are joined together via peptide bonds.c. A protein binds with a substrate, lowering the activation energy of a reaction.d. A protein is exposed to extremely high heat, causing it to lose its secondary structure and be leftwith…