What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K-R-W at pH 8? hint ionizable groups include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K %3D (pКa%3D 10.5) O +2 O -1 O +1

What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K-R-W at pH 8? hint ionizable groups include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K %3D (pКa%3D 10.5) O +2 O -1 O +1

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

See similar textbooks

Related questions

Q: Draw the folded tertiary structure of a polypeptide of at least five amino acids including most of…

A: Structural biochemistry is the discipline of biochemistry concerning the structural elements of…

Q: 2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the…

A: Proteins or peptides are composed of twenty standard amino acids that differ from each other on the…

Q: On the diagram above, draw a line across each peptide bond in oligopeptide 3a. Write the…

A: Since you have asked multiple questions, we will solve the first three question for you. If you want…

Q: The 3° structure of a protein refers to the protein's overall, 3-dimensional shape in space. This…

A: Amino acids are biomolecules that have an amino group, a carboxyl group and a side group that is…

Q: The given protein, Protein X, is a heterotrimer - meaning it is a multimeric protein consisting of…

A: Electrophoresis is the technique of separation of charged molecules under the influence of the…

Q: Hydrogen bond lonic (electrostatic) interaction Hydrophobic interactions Disulfide bond

A: Chemical bonds are necessary for life because they bind molecules together and generate momentary…

Q: At pH-4, what is the net charge of the peptide GKPAD? O+0.5 O-1.0 Oo -0.5

A: The sequence of the given peptide is as follows: Gly-Lys-Pro-Ala-Asp The amino acids are composed of…

Q: Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da)…

A: Gel filtration chromatographic procedure in which the components are separated according to their…

Q: .Here is an oligomeric protein, which has two binding sites: 1)Write the formulas of side chains of…

A: Oligomeric proteins are quaternary structure proteins which possess more than one subunit of…

Q: Answer the below questions based on the following peptide sequence:…

A: Hi! Thanks for your question. The first and the last question will have the same explanation.…

Q: A postgraduate student was given the task of predicting the 1H NMR spectrum for compound A.

Q: Based on the following titration table of Glycine, would you be able to recreate the same for…

A: Glycine is an amino acid. It has a single hydrogen atom as its side chain. It is the one of the…

Q: Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.71; Pk2 = 10.78; PkR = 8.33 His: Pk1 = 1.82; Pk2 =…

A: pK refers to pH at which a particular group is exactly 50% ionized. A tripeptide is a peptide…

Q: Using the generic structure shown, indicate what the substituents are for the structure of…

A: Substituents in the Finerenone-like Molecule:The chemical structure of a generic molecule. To…

Q: Suppose you have a peptide composed of 4 amino acids bonded together: alanine, arginine, asparagine,…

A: Amino acids are the type of biomolecules that form polymers by combining through a peptide bond. The…

Q: 2) For the following amino acids, encircle those with a net charge of -2 at high pH underline those…

A: Alanine, valine, leucine, and isoleucine are hydrophobic amino acids with an alkyl group in their…

Q: Draw the form of histidine (pl = 7.6) that predominates at (i)pH = 7.6 (ii)pH = 10.5 (ii)pH= 5.0

A: Peptides and proteins are the linear chain of amino acids attached via peptide bonds. All-natural…

Q: Describe your first proposed step clearly in words (1-2 sentences) including the buffer/pH used.…

A: Proteins are biomolecules, that is compose of amino acids linked by the peptide bonds. Each protein…

Q: Novel antiviral agents isolated from Caribbean sponges led to the development of vidarabine, the…

A: Vidarabine or 9-β-D-arabinofuranosyladenine (ara-A) is an antiviral drug.

Q: Consider the structure of the tripeptide below. H H₂N-C-C- 0=6 CH₂ CH₂ C=0 1 NH₂ pH 5: O pH 10: H O…

A: The given peptide has three amino acids joined by the peptide bond. There are three ionizable groups…

Q: what does this suggest. b) suggest a macromolecule where this modification might occur

Q: A protein contains three 60-kD polypeptides and six 20-kD polypeptides. Each 60-kD chain is…

A: Electrophoresis means migration of charged particles under the influence of an electric…

Q: What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K at pH 8? hint ionizable…

A: Amino acids are the simplest units for the formation of peptides or proteins. The amino acids are…

Q: Consider the sequences (i-iv) that represent sections of a protein. i) -AEEAAAAMAAAAMAAY ii)…

A: Secondary structure is the formation of regular patterns through interaction between nearby…

Q: Given a peptide chain that is composed of the following amino acids: (branched chain-- polar…

A: Chromatography is a separation technique by which amino acids dissolved in a mobile phase are…

Q: a) Draw a non-covalent interaction between a water molecule and the charge on a phosphorylated…

A: Unlike covalent interactions where there is sharing of electrons between two atoms, in non-covalent…

Q: Consider the following pKa values: terminal amino group: 9.5; C = 8.2; Y = 10.1; K= 10.5; terminal…

A: Isoelectronic point is defined as the pH at which the amino acid does not move in an electric field.…

Q: Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the…

A: Proteins are macromolecules composed of polypeptides which contains more than 20 amino acids. Each…

Q: Helices can be described by the notation nm,where n is the number of residues per helical turn and m…

A: Proteins are a type of macromolecule that have a variety of roles in biological processes. It is…

Q: A protein is purified from a bacterium using Size Exclusion Chromatography (SEC), with a molecular…

A: It is a sieve tube chromatography technique, in which proteins are separated from other proteins…

Q: What would the net charge be of a polypeptide with the sequence M-D-R-N-Q-K at pH 8? hint ionizable…

A: The given polypeptide is M-D-R-N-Q-K M = Methionine D = Aspartic aicd R = Arginine N = Asparagine Q…

Q: list the amino acids that will carry a net charge at pH 7 within a protein. What is the charge at pH…

A: Note : Hi ! Thank you for the question. We are authorized to answer one question at a time. Since…

Q: A 100 mL of 0.1 M amino acid at pH 1.0, whose pKa for the carboxyl group is less than the pKa of the…

A: The amino acids carry different ionizable groups. The ionic form of the amino acids depends upon the…

Q: 1. The graph given represents a size-exclusion chromatogram after the refolding of the hemoglobin…

A: Chromatography is a technique of protein purification in which protein can be separated based on its…

Q: Novel antiviral agents isolated from Caribbean sponges led to the development of vidarabine, the…

A: Due to the increasing viral infections, scientists have discovered some new drugs, having a…

Q: Below is the primary structure of a protein. Вс D R H H H || II || E C - N - с — С — N — С — С — N —…

A: Polypeptides are unbranched, linear polymers that are composed of amino acids linked together by…

Q: IUPAC name for the structure given. (DO NOT write "cis or trans") * ннннн ннн ннннн…

A: Systematic names given to a chemical structure is known as the IUPAC name. IUPAC stands for…

Q: 1) Find the pH of 0.1 M of the differnet forms histidine species. (See image for equation and pKa…

A: Amino acids are building blocks of the proteins. Alpha carbon of amino acids consist of carboxyl…

Q: Titration of alanine by a strong base, for example NaOH, reveals two pk's. Which is the titration…

A: A titration curve of an amino acid is the plot of the pH of the amino acid solution versus the…

Q: Indicate the net charge of cysteine at pH 9.5

A: There are four classes of biological macromolecules- proteins, nucleic acids, lipids and…

Q: What average positive charge of an amino acid side chain with pKa 10.9 at a pH value of 11.9? Answer…

A: Answer :- To calculate the average positive charge of an amino acid side chain with a pKa of 10.9 at…

Q: The pKa of the side chain of histidine is 6.00. What is the percent of protonated histidine at pH…

A: All amino acids contain atleast two ionizable groups- the alpha-amino group and the alpha-carboxylic…

Q: A tetrameric protein dissociates into dimers when the detergent sodium dodecyl sulfate (SDS) is…

A: Proteins are polymers of amino acids linked by peptide bonds. Proteins can be single chain or more…

Q: b) It's said that secondary structures form because of intra- and intermolecular hydrogen bonding…

A: The primary structure of a protein involves the formation of peptide bonds and it is called a linear…

Q: Which of the following statements are False? (i) Parallel b-sheets characteristically distribute…

A: Among the given four statements two were wrong.

Concept explainers

Osmosis

In simple words, osmosis is the slow, gradual movement of a liquid through a membrane. But there are nuances to this process. For instance, there has to be an imbalance in the distribution of solute in the liquid on either side of the membrane, which has to be semipermeable. The liquid in the region with a lower solute concentration moves to the region with a higher concentration, thereby displacing the solution in the process. The objective is to equalize the concentration of molecules on both sides of the membrane; the displacement of liquid can be viewed as a byproduct of this equalization. Since there is no energy required to carry osmosis, it is considered a passive process.

Question

What would the net charge be of a polypeptide with the
sequence M-D-R-N-Q-K-R-W at pH 8? hint ionizable groups
include N-terminus (pKa = 9.0), D (pKa = 3.9), R (pKa = 12.5), K
(pКa %3D 10.5)
O +2
O-1
O +1

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

SEE SOLUTION Check out a sample Q&A here

Step 1: Background

VIEW

Step 2: Answer

VIEW

Step 3: Explanation for incorrect options

VIEW

Step by step

Solved in 3 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.

Similar questions

Within a naturally-occurring polypeptide, under neutral pH conditions (pH = 7.0), which of the following amino acids always has a negatively charged carboxyl group? the first amino acid in the primary structure histidine lysine arginine the last amino acid in the primary structure
The bottom peptide segment is found in the secondary structure composed of anti-parallel - sheets. From the C-terminus of the peptide below, the sequence immediately after alternation contains the following amino acid residues (from N → C) A-F-R-M-Y-A. a) which side do you expect to face the solvent? Briefly explain your reasons NH, но Nterminus
What is the charge on the following peptide at standard biochemical pH? S-Y-D-F-K-I-V-F-L-L +2 -1 0 0 0-2 O +1
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
I wany handwritten solution with full explanation....asap...i will upvote
Of the 20 protein-derived amino acids shown in Table 27.1, which contain Q.) no chiral center
a) The pl of a protein is 9.0. What will be the net charge (positive, negative or neutral) on the protein under the following conditions: A buffer with pH 9.0: A buffer with pH 7.0: A buffer with pH 10.0: b) Your protein is present in a sample buffer which has a pH 7.0. The sample is applied to an ANION EXCHANGE column. Will protein 1 bind to the beads on the column? Yes/No
Select the correct match : 1.Reducing sugar — Sucrose 2.Phosphodiester bond — Between nucleotides on antiparallel strands of DNA 3.Glycosidic bond — Between repeating units of starch and in glycogen 4.Peptide bond — Formed by elimination of H2 between amino acids
Consider the positively charged amino acid lysine Lys2+ 21 COOH I H&N-C-H I pH 14 12 10 8 6 4 2 0 CH₂ I CH₂ I CH₂ I CH₂ T NH₂+ 0 Nelson p85 2.18 = 2.18 PK₁ Lys+ COO™ I H₂N-C-H H₂N-C-H ī I -----) 8.95 Lysº 8.95 pK₂ pka carboxyl = 2.19 pkaamino = 9.67 pka sidechain = 4.25 COO™ I CH₂ I CH₂ I CH₂ I CH₂ I NH₂¹ 1.0 2.0 Equivalents of OH added- COO™ I H₂N-C-H I 10.79 1 10.79 pk Isoelectric point Lys CH₂2 I CH₂ I CH₂ I CH₂ T NH₂ 3.0 +H3N NH3+ T CH₂ T CH₂ CH₂ CH₂ -COO™ H Lysine (Lys, K) Physiological pH = 7.4 < pl → Amino acid is positively charged at physiological pH 1. Consider glutamate in its fully protonated form (e.g. in a pH = 1 solution) 1) Draw all the forms of glutamate at various pH 2) Calculate the pl of this amino acid 3) Sketch a titration curve showing pH as a function of added [OH-] and locate the predominant forms of histidine in the curve STEPS: 1. Find the H atoms that can be removed on the molecule 2. Associated a pka value to each removable H. 3. Draw the Aa structure at:…
A researcher isolates a new protein and finds that it contains 0.755% serine by weight upon amino acid analysis. The molecular mass of serine is 105 g.mol-¹. What is the minimum molecular mass for the protein assuming only one Ser residue per protein molecule? mmin = The researcher estimates the molecular mass of the protein using gel electrophoresis. From this estimated molecular mass, the researcher concludes the protein contains 3 Ser residues. What is the estimated molecular mass of the protein as shown by gel electrophoresis? g.mol-¹ mest = g.mol-1
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys–Pro–Val–Gly–Lys–Lys–Arg-Arg-Pro-Val-Lys–Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-GIn– Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu–Cys-Asp-Pro-Val-Glu–Val–Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu–His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val–Gly–Glu-Glu-Cys-Asp-Pro–Val-Glu–Val–Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu-Val-Tyr-Pro-Asp- Lys–Ala-Gly-Arg-Glu-Ser-Arg-Ala (d) Which of the three peptides would migrate the closest to the anode in isoelectric focusing? (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three…
Which of the following best describes how the secondary structure of a protein is formed? A B с D O=U a-helix H O=C N-H R-C-H C=0 H-N H-C-R O=C N-H R-C-H C=O H-N O-C N-H R-C-H C=O H-N N-H 0= H-C-R H-N C=O R-C-4 N-H O=C H-C-R 4-1 Ç=O R-C-H N-H 0=C H-C-R (=O R-C-H B-pleated sheet ionic bonds between the R groups of the polypeptide amino acids -Uh hydrogen bonds between the carboxyl and amino groups of non-adjacent amino acids covalent bonds between the carboxyl and amino groups of adjacent amino acids hydrogen bonds between the R groups of the polypeptide amino acids