8) A Leu > Ala mutation at a site buried in the core of the enzyme lysozyme ends up being destabilizing. Explain why in terms of AH", AS" (for both the protein and solvent), and AG.
Q: . Most bacterial mutants that require isoleucine for growth also require valine. Why? Which enzyme…
A: A mutation is a permanent alteration in the sequence of nitrogenous bases of a DNA molecule.
Q: A species of bacteria can synthesize the amino acid histidine, so they do not require histidine in…
A: Feedback inhibition is a mechanism to control cellular activity. The activity of the enzyme is…
Q: The first 32 amino acids from the N terminus of the protein bovine angiogenin were determined by…
A: Protein Sequence First of all we need to understand where chymotrypsin act, which bond (peptide…
Q: The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized…
A: The lysozyme is an enzyme found in the secretions like tears and sweat. It cleaves the glycosidic…
Q: The catalytic mechanism of bovine pancreatic RNase A relies upon acid-base catalysis involving the…
A: Bovine pancreatic RNase is a nuclease Enzyme that catalyses the cleavage of RNA. The protein…
Q: What advantages are there for synthesizing an inactive protein that must subsequently be activated…
A: When the proteins are synthesized into naive polypeptide then these are transferred to the…
Q: What would be the expected effect of attaching an ER signal sequence to a cytosolic protein?
A: Free ribosomes in the cytosol synthesize cytosolic proteins as well as proteins intended for the…
Q: What amino acid residue of phosphoglucomutase is able to transfer the phosphoryl group to glucose…
A: The glycogen’s phosphorolytic cleavage produce the glucose-1- phosphate and to enter the metabolism…
Q: Consider the hypothetical serine protease, which shows the specificity pockets. The S, pocket has a…
A: Serine proteases are a family of enzymes that are capable of cleaving peptide linkage of proteins.…
Q: What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue…
A: ATP is adenosine triphosphate and is an organic compound. It is a hydrotrope that provides energy to…
Q: A)How could the sequence of Ala-Met-Thr be distinguished from that of Thr-Ala-Met by tandem ESI-MS?…
A: A polypeptide is a polymer of amino acids. The sequence of a polypeptide is written from the…
Q: In the: Inhibition of splicing by ribozymes Explain: (a) What is the process affected? (b) What is…
A: DNA is the genetic material in most living organisms. It is the information hub of the cell that…
Q: For each of the following genotypes, explain how mutation (identified by a (-) will affect the…
A:
Q: Consider the hypothetical serine protease in the image, which shows the specificity pockets. The S1…
A: Serine proteases are proteolytic enzymes that cleave peptide bonds. They are hydrolases that use a…
Q: The distal Histidine (His 64) in myoglobin is subjected to three different mutations, this is one of…
A: Both hemoglobin and myoglobin are oxygen binding proteins which are found in the red blood cells…
Q: A mutation that changes an alanine to a leucine in the nucleus of a protein leads to a less active…
A: Introduction: Each organism's DNA sequence is unique. Its base-pairs sequence can change from time…
Q: Many blood clotting proteins undergo a post-translational modification in which specific glutamic…
A: Post Translational Modifications (PTM) of such complexity is only observed in eukaryotes and not in…
Q: Consider, for example, that a particular serine residue is phosphorylated to activate the protein.…
A: Phosphorylation can either activate or deactivate a protein. Phosphomimetics replaces amino acids in…
Q: After being stabilized with supplemental oxygen, a blood transfusion, and medication to help with…
A: Hydroxyurea: It is a class of antimetabolites. This class of drug is used to treat cancer. It is a…
Q: I have this strain of e coli. Is P+ o+ Z+ Y+ / I- P+ oC Z- Y+ Will beta-galactosidase and…
A: Lac operon constitutes a set of structural genes regulated by a common promoter in bacteria.
Q: Explain why RNase A cannot catalyze the hydrolysis of DNA.
A: RNase A is a pancreatic ribonuclease enzyme that cleaves single-stranded RNA. It belongs to a large…
Q: Although aminoacyl-tRNA synthetases make few errors, occasionally an error does occur. How can these…
A: Each aminoacyl-tRNA synthetase is highly specific for a given amino acid. It will incorporate the…
Q: In addition to the reactions mentioned in Section 23.5, PLP can catalyze b-substitution reactions.…
A: Pyridoxal phosphate (PLP) is a coenzyme for a variety of enzymatic biochemical reaction. PLP is the…
Q: Why is penicillin such an effective inhibitor of the transpeptidase?
A: Transpeptidase is an enzyme that catalyzes a nucleophillic carbonyl substitution reaction necessary…
Q: Explain why lysozyme cleaves the artifi cial substrate (NAG)4 ~4000 times more slowly than it…
A: Lysozyme is a naturally occurring enzyme found in bodily secretions such as tears, saliva and milk.…
Q: Catalytic residues are often found in loops between helices or strands for increased mobility during…
A: The amino acids that are known to be involved in the chemical reaction catalyzed by an enzyme are…
Q: The BSA precursor protein is 607 amino acids long and has a molecular weight 69.324 kDa. If a…
A: BSA is globular proteins. 1kDa = 1.66 * 10-21 gm The molecular weight of BSA precursor protein is…
Q: Describe the mechanism of action of 1 cycle of the ubiquitin (Ub) ligase system. Describe how the…
A: Introduction Proteins are the essential biomolecules that play a diverse role. Almost all cellular…
Q: When cladosporin acts as an antibiotic working in a bacterial cell, explain the mechanism of action…
A: Cladosporin is a tricyclic octaketide that's a secondary metabolite produced by several fungal…
Q: Once the chains of peptides that make up lysyl-tRNA synthetase protein are synthesized in ribosomes,…
A: Protein folding is the process where the proteins fold themselves to come to their native form. This…
Q: pH will you try to bind lysozyme to a cation exchanger
A: Lysozyme is an antimicrobial enzyme that catalyzes the breakdown of peptidoglycan in the cell wall…
Q: Xylose racemase is a bacterial enzyme that converts the sugar D-xylose to L-xylose, which is needed…
A: Pka of amino acids in the active site changes according to the surrounding environment. Pka increase…
Q: Mutations in the Galactose-1-Phosphate Uridyl Transferase Gene Can you use RFLP to identify this…
A: Mutation --It is an alteration in the sequence of nucleotides in a genome of an organism , virus…
Q: 1. A) Explain this statement, “Most enzymes are gene-encoded proteins, but most enzymes are not only…
A: Enzymes are the catalysts, which are composed of proteins. They help in enzyme catalysis, in which…
Q: If you were to remove the ER retrieval signal fromprotein disulfide isomerase (PDI), which is…
A: We got the information of first type in carboxyl terminus of soluble ER proteins and in golgi…
Q: The structure of adenylate cyclase is similar to the structures of some types of DNA polymerases,…
A: adenylate cyclase DNA polymerases Convert ATP to cAMP Adds dNTP to DNA Plays role in signal…
Q: In most cases, mutations in the core of a protein that replace a smaller nonpolar side chain in the…
A: Cells have aqueous environment that is hydrophilic. So, proteins fold in a way that the hydrophilic…
Q: Lysozyme cleaves between NAG and NAM residues in bacterial cell walls and is, therefore, classified…
A: Lysozyme is a hydrolytic enzyme secreted by lysosomes of eukaryotic cells which are responsible…
Q: Can you answer all the parts to this question please A. Where does a low barrier hydrogen bond…
A: Protease is an enzyme that is observed in both prokaryotes and eukaryotes and is involved in…
Q: "The helix must undergo localized unwinding, and theresulting “open” configuration must be…
A: DNA is the genetic and hereditary material in all living cells (except a few viruses). DNA is passed…
Q: The biosynthetic pathway for the two amino acides E and H is shown schematically in the Figure…
A: Feedback inhibition is a cellular control mechanism in which an enzyme's activity is inhibited by…
Q: What is the role of ATP(CTP): tRNA nucleotidyletransferase?
A: Introduction: A polymerase is an enzyme that creates lengthy polymer or nucleic acid chains. DNA…
Q: 1. Treating (DP) with Flouro Dinitro benzene (FDNB), followed by hydrolysis resulted in the release…
A: Biochemical methods are used for determining the order of nucleotide bases (ATP, GTP, CTP,…
Q: For each of the following genotypes, explain how mutation (identified by a (-) will affect the…
A: The operon is the prokaryotic gene regulatory system that regulates the expression of polycistronic…
Q: Which of the following would be a good chemotherapy approach: blocking formation of the…
A: Cancer is one of the most dreaded diseases of human beings and is a major cause of death all over…
Trending now
This is a popular solution!
Step by step
Solved in 2 steps
- Identify the following by describing their functions: EF-G, EF-Tu, EF-Ts, EF-P, and peptidyl transferaseCan you answer all the parts to this question please A. Where does a low barrier hydrogen bond (LBH) form transiently during the serine protease mechanism? B. What part does this LBH play in the serine protease mechanism?a) At what pH will you try to bind lysozyme to a cation exchanger? b) Is it possible to perform this binding even at a different pH than the one you mentioned in section a? Explain your answer. c) Is it possible to bind lysozyme to an anion exchanger as well? If so, at what pH?
- In the fungus Neurospora, some mutants were obtainedthat lacked activity for a certain enzyme. The mutationswere found, by mapping, to be in either of two unlinkedgenes. Provide a possible explanation in reference to quaternary protein structureIn the serine protease triad, the proximity of an aspartatecarboxylate group to the imidazole group of histidine raisesthe latter’s pKa. Explain.This molecule forms a dimer via pi interactions, resulting to effective molecular stacking. If the molecule can inhibit toxic effects at 0.5mM against gastric carcinoma cells, does it mean that the dimer of this nucleoside analogue will exhibit an IC50 of about 0.25mM?
- Electrophoresis 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.If you were to remove the ER retrieval signal fromprotein disulfide isomerase (PDI), which is normally a sol-uble resident of the ER lumen, where would you expect themodified PDI to be located?Given that a faulty ribosomal protein is the culprit and causes DBA, discuss the possible role of normal ribosomal proteins. Why might bone marrow cells be more susceptible to such a mutation than other cells?
- In a paragraph form, provide the experimental procedures in removal of the carbon dioxide present in the mechanism of reaction of protein that contain native serine residues by the reaction of oxazetidine-containing peptides and α-ketoacidAllosteric Regulation of Ribonucleotide Reductase by ATP and Deoxynucleotides Describe the underlying rationale for the regulatory effects exerted on ribonucleotide reductase by ATP, dATP, dTTP, and dGTP.During SDS-PAGE, glycoproteins migrate as relatively diffuse bands, whereas nonglycosylated proteins typically migrate as narrow, well-defined bands. Explain the reason for this difference in electrophoretic behavior.