The folding and unfolding rate constants for a myoglobin mutant have beendetermined. The unfolding rate constant ke-u = 3.62 x 10-55 andthe folding rate constant ku-p = 255 s1, where Fis the folded proteinand U is the unfolded (denatured) protein. For wild-type myoglobin,AG;u = +37.4 kJ/mol. Which myoglobin is more thermodynamicallystable, the mutant or the wild-type?

Protein folding is a biochemical process in which a random structure protein fold to attain a…

Answered: The folding and unfolding rate…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 10P

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The E1% at 280 nm of the protein myosin is 0.842. You take 40µl of a myosin solution of unknown concentration and add water to a final volume of 2.0 ml. The absorbance of this solution at 280 nm is 0.771. What is the concentration of the undiluted myosin solution? (units = mg/ml).
In active muscle cells, the pO₂ is about 10 torr at the cell surface and 1 torr at the mitochondria (the organelles where oxidative metabolism occurs). Calculate the percentage of bound oxygen transported to the mitochondria of muscle cells by myoglobin (KD = 2 torr). A new oxygen transport protein that exhibits cooperative binding has been isolated and is being studied in the lab. Calculate the Ko value if Y = 0.76 when pO₂2 = 18 torr (assume n = 2.5). How does this compare to the K₂ value for hemoglobin? Does this protein bind more or less tightly to oxygen compared to hemoglobin?
Finally, discuss the consequences of 9.2 uM for actin polymerization in a cell, considering critical concentrations values of 0.1 uM for barbed (plus) end addition and 0.6 uM for pointed (minus) end addition of actin. Recall that at G-actin concentrations above the critical concentration, actin filaments elongate. When the G-actin concentration is greater than the Cc for the barbed end (C (T)) but less than the Cc for the pointed end (Cc (D)), the filament maintains a steady state length due to treadmilling, where the rate of ATP actin addition at the barbed end equals the rate of ADP-actin at the pointed end.
The distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of them: H64N. (Histidine to Aparagine) For the mutation, draw a theoretical binding curve and CO relative to the O2 and CO binding curves for wild-type Mb (see example below). Provide a clear rationale for the binding curve.
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.
After death, muscles become very stiff, a condition known as rigor mortis. Explain the molecular basis of rigor mortis - where in the contraction cycle is the muscle arrested? Why?
Detailed measurements of sarcomere length andtension during isometric contraction in striated muscleprovided crucial early support for the sliding-filamentmodel of muscle contraction. Based on your understand-ing of the sliding-filament model and the structure of asarcomere, propose a molecular explanation for the rela-tionship of tension to sarcomere length in the portions ofFigure Q16–1 marked I, II, III, and IV. (In this muscle, thelength of the myosin filament is 1.6 μm, and the lengths ofthe actin thin filaments that project from the Z discs are 1.0μm.)
The protein fragments ABS1 and ABS2 of tropomodulin were produced as fusion proteins with chitin binding domain and purified by a chitin column. Explain the principles of this type of affinity chromatography and support it with a self‐drawn figure. This is with regards to Tropomodulin/ F-Actin complex.
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 draw the protonic equilibria for the tripeptide what is the IpH?
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 = 9.17; PkR = 6.0 Lys: Pk1 = 2.18; Pk2 = 8.95; PkR = 10.53 draw the protonic equilibria for the tripeptide what is the IpH? What is the dominant structure at pH 2.0? What is the first buffering region of the tripeptide?
Myoglobin stores O2 in muscle tissue to be used by the mitochondria only when the cell is in oxygen debt, whereas hemoglobin can effectively transport O2 from the lungs and deliver it discriminately to cells in need of O2. Describe the structural features that allow these two proteins to accomplish separate functions.
The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.

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