Experimental results describing a protein's amino acid composition are useful for estimating the molecular weight (MW) of theentire protein. A quantitative amino acid analysis reveals that bovine cytochrome c contains 1% tryptophan (M, 204) by weight.Calculate the approximate molecular weight of bovine cytochrome c if there is 1 tryptophan residue. Please enter your answerwith three significant figures.approximate bovine cytochrome c MW:number of threonine residues:19.420.4 x10³Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 9% threonine(M, 119). Calculate how many threonine residues are present in a molecule of bovine chymotrypsinogen. Round your answer tothe nearest whole number.IncorrectIncorrectDa

Proteins are high molecular weight polymers of amino acid residues linked together via peptide…

Answered: Experimental results describing a…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The α-amylase (α-AM) enzyme secreted by Aspergillus has an isoelectric point of approximately 4.2. If the purification method in problem 1 operates at pH 6.5, would the protein carry a positive charge, negative charge, or net zero charge?
Are all the proteins separated properly using two-dimensional (2D) gel electrophoresis? Why or why not?
The last residue of the protein (tail) is Tryptophan, and the first residue (head) is labeled with IAEDANS acceptor. Estimate the length of the protein (head to tail) if the efficiency of RET measures at 0.01 Please show step by step and how to get the 34.014 number
Determine the sequence of the following 10-mer of ferritin using the data below. i. Complete acid hydrolysis of the 10-mer results in identification of 1A, 1D, 1E, 1F, 1H, 1K, 2L, 1T, 1Y ii. Digestion of the 10-mer with chymotrypsin results in 3 fragments containing (D, H, K, T), (F, L) and (A, E, L, Y) iii. Digestion of the 10-mer with V8 protease, which cuts on the C-side of acidic amino acids, results in three fragments containing (D, F, L, Y), (A, E, L) and (H, K, T) iv. Digestion with trypsin results in a fragment H-T and a fragment with all the other amino acids v. Treatment of the 10-mer with FDNB followed by complete acid hydrolysis results in the following two derivatives, DNP-1 and DNP-2 vi. Treatment of the 10-mer with a carboxypeptidase results in a free threonine
Which of the following is NOT a unit of concentration? All of these options are units of concentration. mM Moles/Liter Molar You gathered your data from Lab , and found the following values: Total Activity of lysozyme in HEW: 14 units Total Activity of lysozyme in carb 1: 21 units Total amount of protein in HEW: 70 mg Total amount of protein in Carb 1: 15 mg Calculate the extent of purification of lysozyme in Carb 1. A 7 fold B 150% C 15 fold D 70%
You are working at a major pharmaceutical company, and you have purified an engineered enzyme, and you need to determine the protein stability (kJ/mol). Accordingly, you have collected equilibrium unfolding data using the chemical denaturant urea at 20°C, pH 7.5 and I atmosphere using fluorescence spectroscopy. a) Determine the protein stability (AG [kJ/mol]) via nonlinear least squares (using the available data). b) Write the partial differential equation (i.e., general functional form, variable, constants). c) Describe what would happen to the isotherm if the temperature was increased to 25 °C. Urea [M] 0 0.25 0.5 0.75 1 1.25 1.5 2 2.25 2.5 2.75 3 3.25 3.5 3.75 4 4.25 4.5 4.75 5 FL 340nm 316 315.5 315 314.5 314 315 300 275 225 125 75 60 55 54 53 52.5 52.25 52 51.75 51.5 dG = Vdp-SdT+μA dnд + μB dng dGp = μA dnA+ μg dng A = Folded State B = Unfolded State
A protein of unknown structure has been purified. Size-exclusion chromatography reveals that the native protein has a MW of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of MW 60,000. Chromatography in the presence of 6 M guanidine hydrochloride and 10 mM B-mercaptoethanol yields peaks for proteins of MW 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.
A spheroidal bacterium with a diameter of 1.0 μm (micrometer, 1 μm = 10-6) contains 25,000 molecules of the protein hexokinase. What is the molar concentration of the protein inside the cell?

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