Illustrate the structure of a peptide with the given sequence below at the given conditions. Serine-Threonine-Glutamic Acid-Lysine-Aspartic Acid-Arginine Form with net charge: +3 Dominant form at pH 7
Q: What is the pl for the polypeptide ALRHEN? Use pka of 8 for the N-terminus and 4 for the C-terminus.
A: pI is defined as the the pH of the solution at which the amino acid is present at iso-electronic…
Q: Given pKa values for ionizable groups from Table 27.2, sketch curves for the titration of Q.)…
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Q: indicate which of the amino acid residues in the following peptide sequence contains a group that…
A: When the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing…
Q: A decapeptide undergoes partial hydrolysis to give peptides whose amino acid compositions are shown.…
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Q: A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin;…
A: The sequence of the original peptide has to be deduced.
Q: Estimate the charge of the following oligopeptides at pH 7 based on the pKa values of the…
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Q: Draw the chemical structure of the following amino acid sequence at pH 7, label the peptide bonds,…
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Q: Estimate the pl values of the following peptides: a. Ser-lle and b. Gly-Tyr-Val.
A: The question is based on the concept of biomolecules . we have to calculate isoelectric point for…
Q: +NH3-Gly-Lys-Ser-Arg-COO- (pH=13)
A: At pH = 13 it will have only negative charge at COOH group. Because in basic medium proton is…
Q: QUESTION 1 Use these pKa values to caloulate the charge on the peptide below at pH 6. alpha COOH 2.0…
A: “Since you have asked multiple question, we will solve the first question for you. If youwant any…
Q: Which statement about the peptide G TA is correct? Select an answer and submit. For keyboard…
A: G T A is Glycine Threonine Alanine so option - B contradict option- C also contradict because Asn is…
Q: Consider the pentapeptide Ile-Lys-Asp-Phe-Gly and answer the following (use the pKa values in the…
A: The mentioned pentapeptide is Ile-Lys-Asp-Phe-Gly.
Q: As shown in Mechanism 29.2, the nal steps in the Edman degradation result in rearrangement of a…
A: The given compound thiazolinone is less stable than N-phenyl thiohydantoin and undergoes…
Q: His-Met-Asp-Tyr-Phe-Ser Calculate an approximate pI (isoelectric point) for this peptide.
A: The isoelectric point (pI) is defined as that pH of aqueous solution of amino acids where the…
Q: A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial…
A: So on partial hydrolysis, we will get separate amino acids peptide chain To get our main chain we…
Q: Show where trypsin and chymotrypsin would cleave the following…
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Q: Given the following peptide RISAGDLEVK, Determine the formal charge of peptide a. pH=0.5 b.…
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Q: Consider the partial sequence of a peptide. I L W A N R M S H V L F A V E A Select all amino acid…
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Q: what is the overall charge on the peptide : Pro- Glu-Tyr-Gln-Arg at pH=11
A: A polypeptide or simply peptide is an entity that contains amino acids bonded to each other by…
Q: According to this Ramachandran plot, what is the main secondary structure element found in this…
A: The correct option is:
Q: Show how solid-phase peptide synthesis would be used to make Ile-Gly-Asn.2
A: The first step of solid-phase peptide synthesis to make ile-Gly-Asn is shown below.
Q: For the peptide Ala-Cys-His-Ile-Leu-Asp a. Write the single letter code for the amino acid residues…
A: The questions are based on the concept of biomolecules. a peptide has been given. we have to…
Q: A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin;…
A: To get the sequence of original peptide, we arrange the given fragments one above another according…
Q: ogen pept is rigid, take place about the N-Co and the Co-C bonds in a protein (Co is the a carbon…
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Q: A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial…
A: Phe-Val-Asn-Gln-His, His-Leu-Cys-Gly-Ser, Gly-Ser-His-Leu-Val. The tetrapeeptide fragments formed on…
Q: Consider the pentapeptide Ile-Lys-Asp-Phe-Gly and answer the following (use the pKa values in the…
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Q: Oxytocin, a nonapeptide hormone secreted by the pituitary gland, functions by stimulating uterine…
A: primary sequence of oxytocin
Q: Why is glycine the only amino acid commonly observed in peptides inconformations with phi and psi…
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Q: a) With the help of a schematic diagram describe the synthesis of the tripeptide Phe-Leu- Met using…
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Q: What products are formed when below mentioned peptide is treated with trypsin.…
A: Trypsin: Trypsin cuts the chain from the C -side of the protein chain of lysine and arginine. This…
Q: The important steps in solid phase peptide synthesis are? A) Coupling and hydrolysis B) Hydrolysis…
A: Solid-phase peptide synthesis (SPPS) involves the successive addition of protected amino acid and…
Q: In a variation of the Merrifield solid-phase peptide synthesis, the amino group is protected by a…
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Q: For the peptide sbown below, the pK, of the amino terminal group is 9.00 and 2.00 for the carboxy…
A: Amino acids are the molecules in organic group which contains two functional group that is amine…
Q: The peptide segment shown below is part of a right-handed alpha helix. Please indicate the hydrogen-…
A: There are 4 types of structure of protein- 1- primary 2- secondary 3- tertiary 4- quaternary For…
Q: Taking the structure of the amino acids into account, give a comparative discussion of these pK…
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Q: Indicate which of the amino acid residues in the following peptide sequence contains a group that…
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A: orthinine has a 3 ionizable groups. 1. amino group 2. carboxylic group 3. and a side chain pka of…
Q: Write out the steps for the synthesis of each peptide using the Merrifield method: (a)…
A: a.
Q: What is the name of the peptide below and please give a synthesis for it by using solid phase…
A: The name of the peptide has to be given and a synthesis for it by using solid phase peptide…
Q: Which of the following peptides have a net positive chargeat pH 7? (a) Gly-Ser-Lys, (b) Pro-Leu-Ile,…
A: Among the 20 common amino acids, five have a side chain which can be charged. At pH=7, two are…
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Q: Part B Consider the partial hydrolysis of the peptide Ala-Ser-Gly-Met-Thr-Val. Sort the smaller…
A: In this question, we will see which Peptide will form or not after partial hydrolysis.
Q: Draw the structure of the dipeptide Thr-Cys at pH7. Make sure the following are clearly indicated:…
A: For peptide structure very left one should be N end and very right one should be C end. N end means…
Q: Which has a higher percentage of negative charge at physiological pH (7.4), leucine with pI = 5.98…
A: When an amino acid is placed in a solution which has a pH that is lower than the pI then the amino…
Q: The bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets.…
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Q: Draw the molecule arginyl-alanyl-histidyl-cysteinyl-isoleucyl-asparagine at pH 7. List the name of…
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Q: Suggest a reasonable strategy for the synthesis of the dipeptide Leu-Phe, using established protocol…
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Q: Draw a dipeptide with alanine (R = CH3) at the C-terminus and serine (R = CH2OH) at the N- terminus.…
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Illustrate the structure of a peptide with the given sequence below at the given conditions.
Serine-Threonine-Glutamic Acid-Lysine-Aspartic Acid-Arginine
- Form with net charge: +3
- Dominant form at pH 7
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- Oxytocin, a nonapeptide hormone secreted by the pituitary gland, functions by stimulating uterine contraction and lactation during childbirth. Its sequence was determined from the following evidence: 1. Oxytocin is a cyclic compound containing a disulfide bridge between two cysteine residues. 2. When the disulfide bridge is reduced, oxytocin has the constitution Asn, Cys2, Gln, Gly, Ile, Leu, Pro, Tyr. 3. Partial hydrolysis of reduced oxytocin yields seven fragments: Asp-Cys, Ile-Glu, Cys-Tyr, Leu-Gly, Tyr-Ile-Glu, Glu-Asp-Cys, and Cys-Pro-Leu. 4. Gly is the C-terminal group. 5. Both Glu and Asp are present as their side-chain amides (Gln and Asn) rather than as free side-chain acids. What is the amino acid sequence of reduced oxytocin? What is the structure of oxytocin itself?Deduce the amino acid sequence of an undecapeptide (11 amino acids) from the experimental results shown in the table.Three peptides were obtained from a trypsin digestion of two different polypeptides. In each case, indicate the possible sequences from the given data and tell what further experiment should be carried out in order to determine the primary structure of the polypeptide. a. polypeptide I: 1. Val-Gly-Asp-Lys 2. Leu-Glu-Pro-Ala-Arg 3. Ala-Leu-Gly-Asp b. polypeptide II: 1. Val-Leu-Gly-Glu 2. Ala-Glu-Pro-Arg 3. Ala-Met-Gly-Lys
- A peptide has the following amino acid composition: 2 Met, 2 Phe, 2 Glu, 1 Arg, 1 Lys, 1 Val, 1 Leu, 1 Gly, 1 Ser Reaction of the intact peptide with dansyl chloride followed by acid hydrolysis creates a derivative of Met. A specific cleavage of the intact peptide produces fragments with the following sequences: Fragment A: Glu-Gly-Lys-Phe Fragment B: Met-Ser-Leu-Arg Fragment C: Met-Val-Glu-Phe What information do this result give about the sequence of the peptide? Explain how you arrived on your answer. a) The sequence is: Met-Val-Glu-Phe-Glu-Gly-Lys-Phe-Met-Ser-Leu-Arg b) The sequence is: Met-Ser-Leu-Arg-Met-Val-Glu-Phe-Glu-Gly-Lys-Phe c) The sequence is: Met-Val-Glu-Phe-Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe d) The sequence is: Met-Ser-Leu-Arg-Glu-Gly-Lys-Phe-Met Val-Glu-PheA sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin; the other one was treated with cyanogen bromide. Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn-Thr-Trp-Met-Ile-Lys Gly-Tyr-Met-Gln-Phe Val-Leu-Gly-Met-Ser-Arg Cyanogen bromide treatment Gln-Phe Val-Leu-Gly-Met Ile-Lys-Gly-Tyr-MetThree peptides were obtained from a trypsin digestion of two different polypeptides. indicate the possible sequences from the given data and tell what further experiment should be carried out in order to determine the primary structure of the polypeptide. polypeptide I: 1. Val-Gly-Asp-Lys 2. Leu-Glu-Pro-Ala-Arg 3. Ala-Leu-Gly-Asp
- Which of the following peptides have a net positive chargeat pH 7? (a) Gly-Ser-Lys, (b) Pro-Leu-Ile, (c) Phe-Tyr-Asp.The peptide Proline-Serine-Alanine-Phenylalanine-Glutamine is present at pH 7. Draw the peptide and include stereochemistry.1. A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis.(i) From this information, deduce the primary structure of this polypeptide. Fragments are grouped according to size. Pentapeptide fragments Tetrapeptide fragments Phe-Val-Asn-Gln-His His-Leu-Cys-Gly-Ser Gly-Ser-His-Leu-Val Gln-His-Leu-Cys His-Leu-Val-Glu Leu-Val-Glu-Ala
- Given the following peptideSEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the pKa valuesgiven in Table (b) How many peptides would result if this peptide were treated with(1) cyanogen bromide, (2) trypsin, or (3) chymotrypsin?(c) Suggest a method for separating the peptides produced by chymotrypsintreatment.A tetradecapeptide (14 amino acid residues) gives the following peptide fragments on partial hydrolysis. (i) From this information, deduce the primary structure of this polypeptide. Fragments are are grouped according to size. Pentapeptide Fragments TetrapeptideFfragments Phe-Val-Asn-Gln-His His-Leu-Cys-Gly-Ser Gly-Ser-His-Leu-Val Gln-His-Leu-Cys His-Leu-Val-Glu Leu-Val-Glu-Ala Predict the products formed if the tetradecapeptide is acted upon by trypsin and elastse.Somatostatin is a tetradecapeptide of the hypothalamus that inhibits the release of pituitary growth hormone. Its amino acid sequence has been determined by a combination of Edman degradations and enzymic hydrolysis experiments. On the basis of the following data, deduce the primary structure of somatostatin: 1. Edman degradation gave PTH-Ala. 2. Selective hydrolysis gave peptides having the following indicated sequences: Phe-Trp Thr-Ser-Cys Lys-Thr-Phe Thr-Phe-Thr-Ser-Cys Asn-Phe-Phe-Trp-Lys Ala-Gly-Cys-Lys-Asn-Phe 3. Somatostatin has a disulfide bridge.
