Would the tetrapeptide W-X-Y-Z have the same pl as a peptide Z-Y-X-W? Why or why not?
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Q: amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the…
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Q: Draw Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly peptide. What is the net charge of this peptide at pH 3, 8…
A: polypeptides are made up of amino acids that are joined together by peptide bonds (covalent in…
Q: the peptide (written N-terminal to C-terminal) represented by Ala-Ser-Ala-Tyr the same as the…
A: Ans. Yes, the polypeptide chain of amino acid will be Similarly in structure and function whether it…
Q: In a sample solution given to be analyzed; Starch + Val-Gly-Ile-Trp-Lys-Gly-Ala-Gly-Val-Glu Plan…
A: Peptide bond binds the amino acid together and forms a linear chain ,more than 10 amino acids are…
Q: Draw the structure of following peptide: Glu-Asp-His-Cys-Gly-Arg (B) At pH= 10.7 (A) At pH= 2.1
A: Amino acids are organic compounds having two functional group namely carboxyl and amino. Amino acids…
Q: The peptide below NH-CH- HẠN CH- ČH, -NH-CH- NH-CH- NH-CH- OH CH2 CH2 CH2 HN-ç=NH, NH2 CH2 CH HO-CH,…
A: Amino acids are the building blocks of peptides. The net charge on a peptide depends on the sequence…
Q: How do you think incorporating b-homoserine into a peptide would affect the structure and/or…
A: Homoserine, is the product of a cyanogen bromide cleavage of a peptide by degradation of methionine.…
Q: Write the structure of each of the following peptides. Start with the N-terminal and the COO- on the…
A: Peptides are the sequence of amino acids that are joined through formation of peptide bond. The…
Q: Replacements such as Lysine -- Arginine and Leucine -- Isoleucine usually have very little effect on…
A: Characteristics of amino acids: Amino acids are the nitrogenous monomeric units of biomolecules…
Q: A peptide has the following sequence: Gly-Ala-Lys-Phe-Asp-Met-Val-Pro-Arg-Ala-Leu. What Type your…
A: Proteins are the macromolecule that act as building block of body. It is formed from numerous amino…
Q: Can you please help find the side chain?
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Q: Write the name of the oligopeptide L-E-T-S-P-R-A-Y using their full amino acid names. Draw the…
A: Amino acids are molecules that serve as monomers for proteins. Each amino acid is composed of a…
Q: Would the side chains in the Leu-Thr-Met-Val-Trp-Gly-Pro of a polypeptide be located on the interior…
A: 1.Amino acids that are hydrophobic (water-fearing) in nature are mostly found interior of the…
Q: How many ways can four different amino acids be arranged in a peptide so that each peptide is…
A: Amino acids are organic compounds that contain amine (-NH2) and carboxyl (-COOH) functional groups,…
Q: Draw the structure of the peptide: Val-His-Leu-Thr-Pro-Val-Glu-Lys-Ser-Ala-Val-Thr
A: “Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: PLEASE DRAW the structure of the peptide: Val-His-Leu-Thr-Pro-Val-Glu-Lys-Ser-Ala-Val-Thr and…
A: Amino acids are the biomolecules that are made up of the amino group and a carboxyl group. The amino…
Q: Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet…
A: Amongst secondary structures of polypeptide chains made of amino acids, β-sheets are a more spacious…
Q: For each of the following, would you expect to observe significant a-helical content under the…
A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…
Q: Given the polypeptide chain below: Ala-Arg-Val-His-Asp-Gln Which amino acid/s is/are hydrophobic?…
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Q: raw the complete structure of the tetrapeptide Val-Cys-Glu-Ser.
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Q: Which of the following amino acids is most unlikely to be present in a beta sheet? O Leucine O…
A: Beta sheet consist of beta stands connected by atleast 2 or 3 backbone hydrogen bond laterally which…
Q: Why are amino acids called a-amino acids and why are they designTed as L-form?
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Q: The sequence of a peptide is given below. Ala-gly-val-leu-trp-lys-ser-phe-arg-proWhich peptide…
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Q: Which of the following peptides will likely form a loop or turn in a protein and explain why
A: The turns are the third type of secondary structure. These are short, U-shaped secondary structures,…
Q: Consider the peptides Ser-Glu-Gly-His-Ala and Gly-His-Ala-Glu-Ser. How do these two peptides differ?
A: Introduction: The organic molecules that contain two functional group that is amino and carboxyl are…
Q: Draw peptide Pro-Ser-Ala-Phe-Glu as you would see it at pH 7. Include stereochemistry.
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Q: How many peptide bonds in this peptide chain LEU-ILE-LEU?
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Q: Pro-Ser-Ala-Phe-Glu. Draw this peptide at pH 7 and include its stereochemistry.
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Q: A polypeptide has a high pI value. Suggest which aminoacids might comprise it
A: A polypeptide chain having a high pI value comprise of following amino acids : Lysine, arginine.
Q: _____________ are degrons with sequences containing proline, glutamate, serine, and threonine…
A: Peptides are chain of amino acids containing few amino acids. The amino acids are attached with…
Q: What is the net charge at pH 7 on a peptide with the following sequence?…
A: Amino acids are the building blocks of proteins which are composed of amino group (NH3+), carboxyl…
Q: draw the structure of the tripeptife Pro-Ser-Cys as it would appear at physiological PH with its…
A: Amino acids can be polymerized to form chains. Peptide bond formation is a condensation reaction in…
Q: Identify and encircle the peptide bonds in this polypeptide (Asp-Sec-Leu-Cys-Glu).
A: Amino acids are compounds that contain amino as well as carboxylic acid groups. These are the…
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Q: You have isolated the following peptide: His-Ser-Arg-Ala-Glu-Leu-Pro-Gly A) Calculate the…
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Q: Indicate whether each of the following amino acids is polar: a. lysine b. tyrosine c. leucine d.…
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Q: A peptide has the following sequence: Gly-Ala-Lys-Phe-Asp-Met-Val-Pro-Arg-Ala-Leu. What is the net…
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Q: Draw the peptide formed between asparagine and histidine. H,N-CH-ċ-OH H,N- -CH—С—он CH2 ČH2 N° NH2…
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Q: you have the following peptide Arg-Ile-Pro-Leu-Asp-Lys-Glu The net charge on this peptide at pH 7.0…
A: Amino acids are biomolecules that are comprised of two functional groups, these are an amino group…
Q: Assign IUPAC names to each of the following small peptides.Gly-Ala-Leu…
A: The international union of pure and applied chemistry (IUPAC) name of a peptide refers to the full…
Q: At what pH can you separate the following peptides: ala-ala-ala glu-glu-glu, his-his-his? A. 2.0 B.…
A: Isoelectric focusing is a type of electrophoresis in which proteins or peptides are separated on the…
Q: A peptide has the sequence Glu-His–Trp–Ser-Gly-Leu-Arg-Pro-Gly The pK, values for the peptide's side…
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Q: In the peptide Ser-Cys-Ala-Gly, the N-terminal end is glycine. O cystein. O serine. Oalanine.
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Q: The peptide cys-leu-glu-ala-cys-lys is at pH 7 in oxidizing conditions. Part a) Draw the peptide's…
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Q: What is the overall net charge on the peptide
A: Given peptide: lys-lys-ser-glu pKa of amino group (lys) = 9.6 pKa of carboxyl group (glu) = 2.1 pKa…
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- What does this important observation imply about the relation between the amino acid sequence of insulin and its three-dimensional structure?Which of the 20 “standard” amino acids are (a) purely glucogenic, (b) purely ketogenic, and (c) both glucogenic and ketogenic?Which of the following statements about the transamination and deamination steps of amino acid degradation is true? (A) a-ketoglutarate is always formed during a transamination between an amino acid and glutamate. (B) Transamination reactions produce glutamate that is deaminated after entering the urea cycle. (C) Free ammonia is removed from glutamate using glutamate dehydrogenase and NAD+ as an oxidizing agent. (D) The free NH4+ that is removed from glutamate during the deamination reaction is used to form glucose.(E) The carbon backbone that results from transamination enters the mitochondria to be used in the urea cycle.
- What is the relationship between -ketoglutarate, glutamate, and glutamine in amino acid anabolism?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.If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work? Do not just say yes or no. Give a short explanation for this hypothetical situation.
- Describe the structures of glutamine and alanine. What are the characteristics of the R-groups? What other features of these amino acids make them important as they relate to metabolism?The sucrose substitute tagatose is produced by hydrolyzing lactose and then chemically converting one of the two resulting aldoses to a ketose. Which residue of lactose gives rise to tagatose?Draw the chemical structures resulting from the transamination of the following amino acids: a. Aspartic acid + alpha-ketoglutarate à ______________ b. Glutamic acid + pyruvate à ______________________ c. Alanine + alpha-ketoglutarate à ___________________ d. Phenylalanine + pyruvate à ______________________ e. Serine + alpha-ketoglutarate à ____________________
- Can an amino acid be both glucogenic and ketogenic? Explain why or why not.Will an amino acid be glucogenic or ketogenic if it is catabolized to the following molecules?(a) Phosphoenolpyruvate(b) -Ketoglutarate (c) Succinyl-CoA(d) Acetyl-CoA(e) Oxaloacetate(f) AcetoacetateBriefly discuss why each of the three common forms of galactosemia involves impaired utilization of galactose. Which metabolic process is blocked in each condition?