describe a detailed experimental procedure for the chemical synthesis of proteins with the α-ketoacid hydroxylamine (KAHA ligation), using (S)-5-oxaproline (Opr) as a key building block.
Q: Please provide a chemical explanation for why the addition of water across the double bond is…
A: Metabolism is the chemical reactions that occur in cells and organisms. It involves catabolism and…
Q: Write a balanced equation for the synthesis of TMP from dUMP that is coupled to the conversion of…
A: Biomolecules are organic molecules that occur in living systems. Biomolecules include carbohydrates,…
Q: Under certain conditions, peptide bond formation rather than peptide bond hydrolysis is…
A: Peptide bond formation- A peptide bond is a chemical bond formed between two molecules when the…
Q: Draw in detail the pathway of de novo synthesis of deoxythymidine phosphate and provide a brief…
A: First carbamoyl phosphate is synthesized , which then enters the de-novo synthesis pathway for…
Q: Write a balanced equation showing peptide bond formation between threonine and aspartate.
A: Peptide bond is the bond which was formed between two amino acids where the carboly terminal of one…
Q: Propose a method to determine the size and basic structure of chymotrypsin for the purpose of…
A: Any matter on the planet consists of atoms linked by interatomic bonds. The properties of the matter…
Q: Under certain conditions, peptide bond formation is more thermodynamically favorable than peptide…
A: Amino acid is the monomer of proteins. When several amino acids combine, they form protein. The bond…
Q: Explain why methotrexate inhibits the synthesis of histidine and methionine.
A: Competitive inhibition is the competition between a substrate and inhibitor that compete for the…
Q: Write the mechanism (in detail) for the conversion of aspartate and carbamoyl phosphate into N -…
A: Aspartate carbamoyl transferase helps in the initial step of biosynthetic pathway of pyrimidine…
Q: Name the heterocyclic substituent found in the molecule shown according to the general type of…
A: A cyclic compound containing a ring structure that has atoms from different elements (at least 2)…
Q: Propose a reaction mechanism for the condensation of an acetyl unit with a malonyl unit to form an…
A: Fatty acid synthesis takes place in the cytoplasm. where fatty acid synthesis occurs in two phases.…
Q: What is the biochemical rationale for the isomerization of glucose 6- phosphate to fructose…
A: Glycolysis is a metabolic pathway in every cell. In this process glucose is broken down into 2…
Q: Write a balanced equation for the synthesis of sn-1-stearoyl-2- oleylglycerophosphorylserine,…
A: Phospholipids are lipids containing two fatty acids, glycerol, and a head group (serine, choline,…
Q: An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide…
A: Protein disulfide isomerase or PDI is an enzyme that breaks sulfide bonds and is found in the…
Q: Draw the tetrapeptide Met-Ile-Lys-Glu at a ph of 12?
A: The pKa values of amino acid side chains play an important role in determining the pH-dependent…
Q: Draw structural formulas for the products obtained when the tripeptide Thr-Leu-Ile undergoes…
A: An amino acid is a chemical molecule that serves as a building block of proteins. There are 20…
Q: Describe the importance of Haworth and Fischer projections on sugars like pentoses and hexoses?
A: --Fischer projection is the 2D representation of an organic molecule by projection . This is mainly…
Q: If thymine nucleotides are degraded by the same enzymes as those catabolizing uridine nucleotides,…
A: The cleavage of the ring structures metabolizes thymine and uracil nucleotides. The usual end…
Q: - Keto counterparts. Name the a-ketoacida-ketoacid that is formed by the transamination of each of…
A: Tranamination is a reaction in which the amino group of an amino aid is transferred to an…
Q: What is the oligosaccharide-transferring moiety in N-link glycosylation?
A: N-linked glycosylation, is the attachment of an oligosaccharide, to a nitrogen atom mostly of the…
Q: Sketch a titration curve for the amino acid cysteine, and indicate the pKavalues for all titratable…
A: Cystine is a proteogenic amino acid that has a thiol side chain. The thiol group of cysteine is…
Q: Briefly discuss the synthesis of selenocysteine amino acid.
A: Selenocysteine(Sec): It is the 21 st amino acid of the genetic code and this amino acid contains…
Q: Draw the structure of the polyketide you would expect to obtain from one unit of acetyl coenzyme A…
A: Polyketides: These belong to a very large class of molecules that includes molecules that are…
Q: indicate at the structural level how 3TC works as a deoxycytosine analog, and why it is a chain…
A: The synthesis of a DNA molecule from the double stranded DNA template by the enzyme DNA polymerase…
Q: Explain why the indole nitrogen of tryptophan is more weakly basic than one of the imidazole…
A: Histidine contain imidazole ring which does not show resonance. Tryptophan is an aromatic amino…
Q: . Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate…
A: Glutamate-1-semialdehyde 2,1-aminomutase is an enzyme which belongs to the family isomerases;…
Q: N -Acetylglutamate is required as a cofactor in the synthesis of carbamoyl phosphate. How is…
A: N-acetyl (NAG) glutamate is considered as a cofactor, in the synthesis of the carbamoyl phosphate,…
Q: What is the catalytic triad of chymotrypsin? Describe the mechanism of chymotrypsin in cleaving a…
A: Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum, where it…
Q: Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme…
A: Transition state structural analogs of enzymes are chemicals with a structure that resembles the ES…
Q: With the aid of the simple generic diagram, identify and explain how the type of chemical bonding…
A: An alpha helix is a periodic secondary structure in proteins. This secondary structure is stabilized…
Q: 19.25 Write structural formulas to represent the formation of the two dipeptides that form when…
A: The proteins form a class of biological macromolecule and are composed of alpha amino acids. There…
Q: Why is it reasonable to expect that glucose6-phosphate will be oxidized to a lactone (see Question…
A: Glucose-6-phosphate is a compound of glucose that is an ester chemically. It is a phosphorylated…
Q: In a paragraph form, provide the experimental procedures in removal of the carbon dioxide present in…
A: Proteins are composed of amino acids in which amine group of one amino acid linked to carboxyl group…
Q: Explain the biochemical defect that leads to Lesch-Nyhan syndrome and suggest how the defect might…
A: Introduction: Purines (adenine and guanine) and pyrimidines (cytosine, thymine, and uracil) play…
Q: Show the steps involved in a Merrifield synthesis of Phe-Ala-Val.
A: In the Merrifield solid phase method, the synthesis of peptide is forwarded with the growing amino…
Q: In the pyrimidine degradative pathway, all pyrimidines undergo conversion to uracil, which undergoes…
A: Pyrimidines are one of the two classes of heterocyclic nitrogenous bases found in the nucleic acids…
Q: Illustrate and explain the difference between α-D-glucopyranose and β-D-glucopyranose structures.
A: Glucose is the most abundant monosaccharide which was composed of the molecular formula C6H12O6 . it…
Q: What type of protein structure does the active form of Catechol-oxidase most likely possess?
A: Catechol oxidase is a copper oxidase and contains a type 3 di-copper cofactor. It catalyzes the…
Q: Most bacterial mutants that require isoleucine for growth also require valine.Why? Which enzyme or…
A: Mostly the bacteria that require the isoleucine amino acid for growth also requires valine. This is…
Q: Identify all the possible products when the tripeptide Ala-Val-Ala undergoes partial hydrolysis
A: Proteolytic enzymes hydrolyze proteins at optimum temperature and pH and cleaves bonds between them.…
Q: Based on the pk table for amino acids (Table 1.1), draw the structures with net charge, and the…
A: Acid strength is the tendency of an acid to dissociate and donate a proton. The value of pKa of an…
Q: Using the following data, determine the correct sequence of the octapeptide. Edmund's Reaction =…
A: Chains of Amino acids are held together through a peptide bond to form a structure known as…
Step by step
Solved in 2 steps
- Show the steps involved in a Merrifield synthesis of Phe-Ala-Val.From the peptide chain: Met-Tyr-Phe-Arg-Ile-Glu-Asn-Asp-Ser, draw the structure of the product formed when reacted with ElastaseD-Talose is a C2 epimer of D-galactose. Using the Fischer projection structure, draw the product of reaction ofD-talose with the given reagent or enzyme and write the systematic name of the product. 1. 2,4-DNP 2. Reaction with aminotransferase and then acetyltransferase at C4
- Draw the following sugars using Haworth projections:a. b-d-galactopyranose b. a-d-tagatopyranose c. a-l-glucopyranoseDevise a solution-phase synthesis of Ala-Leu-Val-Phe-Met, starting from the requisite Boc-protected amino acidIn 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-ketoacid
- Under certain conditions, peptide bond formation rather than peptide bond hydrolysis is thermodynamically favorable. Would you expect chymotrypsin to catalyze peptide bond formation? Explain.Based on your knowledge of the natural amino acids, what would you expect pKa of the sidechain of beta-(aminomethyl)succinic acid to be? Draw an appropriate titration curve for beta-(aminomethyl)succinic acid, labeling the axes, indicating the equivalence points and the pKavalues, and use a drawing to show the protonated/deprotonated forms.Name and draw the structure of the a-keto acid resulting when each of the following amino acids undergoes transamination with a-ketoglutarate: (a) aspartate, (b) glutamate, (c) alanine, (d) phenylalanine.