Concept explainers
The folding and unfolding rate constants for a myoglobin mutant have been determined. The unfolding rate constant
Want to see the full answer?
Check out a sample textbook solutionChapter 8 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
- Calculate the K of A given K₁ = HA(aq) + H2O(l) = H3O+ (aq) + A¯¯(aq) K = 5.90×108arrow_forwardHeart and muscle cells, where myoglobin resides, maintains an intracellular pO2 of about 2.5 torr. Calculate the fractional saturation (for human myoglobin) if a small change (1 torr) in oxygen partial pressure occurs in either direction (ie what happens at 1.5 torr, what happens at 3.5 torr?) and explain how a small change in oxygen pressure dramatically changes the myoglobin oxygen binding.arrow_forwardGiven 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?arrow_forward
- 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?arrow_forwardProtein 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.arrow_forwardIn a rat cardiomyocyte, the levels of creatine, phosphocreatine, and free phosphate were found to be 37.6mM, 40.3mM, and 8.02mM, respectively. Given that the standard free energy change is –43.0 kJ/mol, what is the true free energy change for phosphocreatine hydrolysis in the cardiomyocyte described above?arrow_forward
- Two co-op students at your start-up company have been asked to evaluate the rate of reaction occurring in a transparent gel particle containing immobilized mouse melanoma cells. The equation for the reaction rate ris is: Vmax T'As Km+CAs where R=3.2 mm, Vmax= 0.12 gmol s' m3, CAS = 41 gmol m3, and Km=0.8 gmol m3. One student reports a reaction rate of 1.6x10 gmol st; the other reports 1.6x10 1º gmol s1. You left your calculator on the bus this morning, but must know quickly which student is correct. Use an order-of- magnitude calculation to identify the right answer. Which student is correct?arrow_forwardFinally, 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.arrow_forwardSickle cell anemia is caused by a point mutation in the β-globin chain of hemoglobin. Glutamic acid is replaced by Valine. HBB sequence in normal adult hemoglobin (Hb A): Leu-Thr-Pro-Glu-Glu-Lys-Ser HBB sequence in mutant adult hemoglobin (Hb S): Leu-Thr-Pro-Val-Glu-Lys-Ser What effect does this mutation have on the structure and function of the protein? Predict what would happen to the RBC if the glutamic acid was replaced with asparagine instead of valine.arrow_forward
- The enzyme lysozyme kills certain bacteria by attacking a sugar called N-acetylglucosamine (NAG) in their cell walls. At an enzyme concentration of 2 × 10-6 M, the maximum rate for substrate (NAG) reaction, found at high substrate concentration, is 1 × 10-6 mol L¯'s1. The rate is reduced by a factor of 2 when the substrate concentration is reduced to 6 x 10-6 M. Determine the Michaelis-Menten constants Km and k, for lysozyme.arrow_forwardElectrophoresis is performed at PH 6.8 on a mixture of mutated hemoglobin that differ from normal haemoglobin (Hb) only by the substitution of one amino acid- Hb X: Val replaced par Glu - Hb Y: Asp replaced by Leu - Hb Z: Glu replaced by Lys What will be the order of migration between cathode and anode of these mutated Hb compared to normal Hb? Justify your answer.arrow_forwardCalculate the solubility of Ag,CO3 (in mol/L) at 25 °C in a 0.02 M Na2CO3 solution. Hint: Ag,CO3(s) → 2Ag*(aq) + co3?(ag) Ksp (Ag,CO3) = 8.1 x 10 12 NażCO3(aq) → 2Na*(aq) + CO3 (aq)arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON