Calculate the isoelectric point for the dipeptide Asp-Arg. Use the pKa table available on Latte. isoelectric point =

Q: Use the values provided below to calculate the predicted isoelectric point, pl, value for aspartame…

A: Isoelectric point:  Isoelectric point of a amino acid is the pH at which amino acid has a neutral…

Q: Shown are the configuration of a gel electrophoresis experiment. Charged plates establish an…

A: Gel electrophoresis is useful in the separation of DNA fragments on the basis of charge and its…

Q: 25.) The area indicated by the arrow is the A) sugar-phosphate backbone B) minor groove C) major…

A: The correct option to this is:

Q: What is the greatest barrier to development of fusionreactors?

A: Nuсleаr  fusiоn  is  the  рrосess  in  whiсh  twо  light  nuсlei  соmbine  tо  give  heаvier…

Q: Marie: The cell lines produce recombinant FIX and other proteins. Which biomolecule can specifically…

A: The biomolecule that can detect the presence of FIX in a full sample of other proteins: a).…

Q: Consider a peptide: Glu-Glu-His-Trp-Ser-Gly-Leu-Arg-Pro-Gly-His If the pKa values for the…

A: If the pH of the solution is greater or equal to the pKa of side chain then the side chain will be…

Q: 5 ased on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 97.4 kDa and…

A: Given , molecular weight of (no beta -Me ) purified sample = 97.4 kDa molecular weight of (beta -Me)…

Q: select

A: 1- At this point, Protein exciting in Zwetterion form means this will contains equal amount of…

Q: alculate the Ksp for uraninite (reaction 1) and rutherfordine (reaction 2).             UO2 + 4 H+…

A: UO2+4H+ →U4+  + 2H2O Ksp = U4+Ksp = S Reaction  :1 Ksp  = S

Q: The structure of haemoglobin: A. has an alpha-beta architecture. B. is a hetero tetramer. C. is a…

A:

Q: The amino acid His is triprotic with pK1 (α-COOH) = 1.82, pK2 (α-NH3+) = 9.17, and pK3 (side chain)…

A: If the pKa of acid is equal or lower than the pH of the solution then the acid will get deprotonated…

Q: 7. In the biosynthesis of proteins it is important that the correct tRNA binds to its corresponding…

A:

Q: Please create the titration curve of aspartate and annotate the corresponding isoforms.

A: Amino acids are amphoteric in nature due to the presence their ionizable α-amino and α-carboxylic…

Q: B. Show the structure of the following amino acids where the Zwitterion formed and calculate the pl.…

A:

Q: Give the numbers of peptide bond present in given structure, structure is given at pH 10.5,  find…

A: The CO- NH bond is called peptide bond. A peptide bond connects two Amino acid units. Amino acid…

Q: MAVA=MBVB.

A: Preparation of a less concentrated solution from a more concentrated solution by adding solvent is…

Q: Consider the hypothetical serine protease in the image, which shows the specificity pockets. The S,…

A: Hydrophobic side chains are non-polar side chains. The hydrophilic side chains are polar, acidic,…

Q: Choose true or false. Increase in temperature during ITC experiments can be used to determine the…

A: Introduction: ITC stands form Isothermal Titration Calorimetry. The technique is used to study the…

Q: 10. Draw the full chemical structure of the tetrapeptide G-H-F-A as it would look at pH 12.0. Use…

A:

Q: The isoelectric point (pl) of a peptide is the pH at which the Group pK peptide ceases to migrate in…

A:

Q: If the pl for asparagine is 5.43, draw the structure at a pH of 9.5?

A: The pl for asparagine = 5.43 pH = 9.5

Q: Answer Q21, 22, 23

A: 21. Third statement is not correct. [Zn(NH3)4]+2  is sp3 hybridized. Vanadium has 5 valence…

Q: 4mL of diluted protein solution was prepared by mixing 200uL of the protein solution with 3.8mL of…

A: Lysozome activity = -0.080 (abs/min)

Q: The polypeptide LMKYTNMRLEDTRYND is hydrolyzed by trypsin for sequencing. This will result in how…

A: Proteins are polypeptides, polymers made up of a large number of amino acids joined together by…

Q: Calculate the isoelectric pH of this peptide: His-Tyr

A: Here we are required to find the isoelectric point pH of the peptide.

Q: Two phenylalanine residues are separated by 1.0 nm in a polypeptide. Calculate the dispersion…

A: Dispersion force is the force of attraction that exist between atoms or molecules that developed…

Q: 75mL of a 0.2M solution of a tripeptide Ser-Cys-His is adjusted to pH=8.6. The solution is then…

A: The explanation is given below-

Q: Calculate the volume, in liters, of 1.666 M KOH that must be added to a 0.129 L solution containing…

A: The given data contains, mass of glutamic acid hydrochloride = 9.42 g. Molar mass of glutamic acid…

Q: Given the following peptideSEPIMAPVEYPK(a) Estimate the net charge at pH 7 and at pH 12. Assume the…

A:

Q: 17. H,N-CH-C-NH-CH, -COOH À BC D Ė Where is the peptide linkage in the dipeptide above? a. A Ob. B…

A: A peptide bond is a chemical bond formed between two molecules when the carboxyl group of one…

Q: 50 mL of a 0.1M solution of tripeptide His-Arg-Ala is adjusted to its isoelectric point (pI). The…

A: Given: 50 mL of a 0.1M solution of tripeptide His-Arg-Ala. i) The solution is then titrated with 150…

Q: The amino acid (S)-alanine has the physical characteristics listed under the structure. What is the…

A: Enantiomers are the stereoisomers which are nonsuperimposable mirror image of each other. All the…

Q: The force constant katr of a backbone Ca – -C bond in a peptide is 250.0 kcal/mol/Angstrom² and the…

A: Given: Force constant (kstr) of bond = 250 Kcal/mol/Angstrom2  Equilibrium bond distance (r0) = 1.49…

Q: 6) If we represent protein folding with the following equilibrium expression: Unfolded protein=…

A: Folded Protein - Protein folding is the process of shrinking a polypeptide chain into its original…

Q: Dutline the steps used to find values for a BLOSUM amino acid similarity matrix.

A:

Q: Alpha-helices and beta-sheets are part of. structure in proteins. O tertiary O quaternary O…

A: Hi, since you have posted multiple questions we will answer the very first question for you. kindly…

Q: Consider the hypothetical serine protease in the image, which shows the specificity pockets. The Si…

A: The nonpolar side chains are known as hydrophobic. The polar, acidic, and basic side chains are…

Q: Aspartate has three ionizable groups with pKa values of 1.88, 9.60, and 3.65. What is the average…

A:

Q: IIUne UI the above äre true 4. What is the starting point for selection of a suitable ion-exchange…

A: Proteins (or any biomolecules) are separated using ion-exchange chromatography based on changes in…

Q: The amino acid histidine has a side chain for which the pKa 6.0. Calculate what fraction of the…

A: from Henderson Hasselbach equation we have pH = pka + log [conjugate base] /[ acid form] acid form…

Q: This technique uses the principle of isoelectric point to separate a mixture of proteins into its…

A: 1. Electrophoresis : Neutral amino acid contains one -COOH and one -NH2 groups. Hence, they exist as…

Q: 10. Draw the full chemical structure of the tetrapeptide G-H-F-A as it would look at pH 12.0. Use…

A: We have to predict the structure of peptide at pH of 12

Q: What is the pI for the polypeptide ALRHEN? Use pKa of 8 for the N-terminus and 4 for the C-terminus

A:

Q: Assume a pH gradient of 4.0 units across a thylakoid membrane, with the lumen more acidic than the…

A: Experimental temperature = 25 o C The wavelength of photon= 650 nm     The given efficiency       =…

Q: A direct current was passed through a solution containing valine histidine and aspartic acid at a pH…

A: When the electricity is passed, the amino acids move based on their charge.

Q: what is the role of Cu+2 ion in biuret test for proteins?

A: Biuret test is used to detect the presence of peptide bonds in a molecule.

Q: What is the percentage of the negatively-charged species of the tripeptide Val-Leu-Ser at pH 7.0?

A: At pH = 7, the carboxyl terminal will have a full -1 charge. At pH = 7, we need to use…

Q: 4. Another peptide fragment that is 33 residues long is recognized as the most resistant to being…

A: In the given sequence of peptide, L, Q, P, F, and Y are five different amino acids.

Spectroanalytical Methods

Spectroanalytical methods measure the wavelength and intensity of radiations that are either emitted or absorbed by a molecular or atomic species. These methods are useful for evaluating the electronic or atomic arrangement of the molecules of a given analyte.