Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovine pancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity when heated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the native structure and function of the protein. please do not copy from other answers here
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Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovine
pancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity when
heated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the native
structure and function of the protein.
please do not copy from other answers here
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- Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein.Globular proteins with multiple disulfide bonds must be heated longer and at higher temperature to denature them. Bovinepancreatic trypsin inhibitor (BPTI), having 58 amino acids in a single chain and 3 disulfide linkages, loses its catalytic activity whenheated at nearly 90°C for 5-10 minutes. Explain the molecular basis of this observed thermal property of BPTI relative to the nativestructure and function of the protein. do not coy from other answers hereExperimental results describing a protein's amino acid composition are useful for estimating the molecular weight (MW) of the entire protein. A quantitative amino acid analysis reveals that bovine cytochrome c contains 17% lysine (M₁ 146) by weight. Calculate the approximate molecular weight of bovine cytochrome c if there are 18 lysine residues. approximate bovine cytochrome c MW: Da Bovine 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 to the nearest whole number. number of threonine residues:
- Experimental results describing a protein's amino acid composition are useful for estimating the molecular weight (MW) of the entire protein. A quantitative amino acid analysis reveals that bovine cytochrome c contains 2% methionine (M₁ 149) by weight. Calculate the approximate molecular weight of bovine cytochrome c if there are 2 methionine residues. approximate bovine cytochrome c MW: Da Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 9% glycine r (M, 75.1). Calculate how many glycine residues are present in a molecule of bovine chymotrypsinogen. Round your answer to the nearest whole number. number of glycine residues:Experimental results describing a protein's amino acid composition are useful for estimating the molecular weight (MW) of the entire 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 answer with three significant figures. approximate bovine cytochrome c MW: number of threonine residues: 19.4 20.4 x10³ Bovine 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 to the nearest whole number. Incorrect Incorrect DaSome 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.
- Experimental results describing a protein's amino acid composition are useful for estimating the molecular weight (MW) of the entire protein. A quantitative amino acid analysis reveals that bovine cytochrome c contains 2% methionine (M, 149) by weight. Calculate the approximate molecular weight of bovine cytochrome c if there are 2 methionine residues. approximate bovine cytochrome c MW: Da Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 9% glycine (M, 75.1). Calculate how many glycine residues are present in a molecule of bovine chymotrypsinogen. Round your answer to the nearest whole number. number of glycine residues:The equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.
- Give the molecular basis of the observed mechanical properties of glutenin, a wheat storage protein rich in disulfide linkagesand responsible for the cohesive and elastic characteristics of dough made from wheat flour. Use not more than 10 short sentences for this item.Asp residue (both of which are essential for catalysis) with pK, values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction? Explain your reasoning. (Carboxypeptidase Y (CPY) contains ten cysteine residues that form five disulfide bonds in the native structure of CPY. Suppose CPY is reduced and unfolded in urea.Part AIf the reduced unfolded protein were oxidized prior to the removal of the urea, what fraction of the resulting mixture would you expect to possess native disulfide bonds?Express your answer using three significant figures.