Draw the form of histidine (pl = 7.6) that predominates at (i)pH = 7.6 (ii)pH = 10.5 (ii)pH= 5.0
Q: Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid…
A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…
Q: What forces of attraction hold the subunits in a quaternary structure?
A: Protein play wide variety of essential function in our body. They provide strength and structural…
Q: What is the biologically-preferred stereochemistry and ionization states for the pentagon-peptide…
A: Proteins are one of the major biomacromolecules. They are primarily composed of polypeptide chains .…
Q: You have prepared a BSA serial dilution (ug ml) to construct a protein standard curve, for which the…
A: The standard equation for calculating concentration is Beer Lambert's law, A= ebc, where A is…
Q: Of the following choices, which one is NOT a component of nucleotides?
A:
Q: Which nuclear isotope used in protein NMR spectroscopy is the most sensitive to detect? Briefly…
A: NMR Spectroscopy is used to study the structure and composition of biomolecules like proteins. Here…
Q: Refer to the following titration curve below: 13 12 11 10 9 7 4 2 4 6 8 10 12 14 16 18 20 22 24 26…
A: Amino acids are the basic units of proteins. The amino acids are combined by a peptide bond that…
Q: Calculate the net charge of the following peptide sequence DAVIRSAXSUEY at pH 7 а. -1 b. -2 с. -3 d.…
A: This peptide contain D, H and E as charged amino acids. all the ionizable groups present in the…
Q: Below is the titration of histidine. Calculate the average charge of histidine at pH 6.50. ÇOON…
A: Hi! Thank you for the question, as per the honor code, we are allowed to answer the first…
Q: Why are salt bridges (ionic interactions) in proteins sensitive to pH?
A: Salt bridges : A salt bridge or ion bridge in electrochemistry, is a laboratory device used to…
Q: Which is more likely to be changed by heating a protein, its primary structure or its tertiary…
A: When heating of the protein is done then primary structure of the protein does not get changed or…
Q: The pKa of the side chain imidazole group of histidine is 6.0. what is the ratio of uncharged to…
A: Amino acids are the monomeric units of proteins. There are 20 amino acids occurring in nature. Amino…
Q: What is the net average charge on the predominant form of lysine at pH values of (a) 2.0, (b) 5.0…
A: Amino acids are organic compounds having carboxyl group and amino group. At extreme low pH, amino…
Q: In regards to the protein structure, explain what is meant by “tertiary structure.” What are the…
A: There are four levels of protein structure are important to attain the final 3- dimensional folded…
Q: Draw the structure of the same tripeptide at pH 7.00.
A: The pKa values of amino acid side chains, the pKa of the alpha amino group at the N-terminus and the…
Q: Estimate the molecular weight of a B-a-B supersecondary element that is 3 nm high?
A: Supersecondary structures (also called motifs ) are characteristics folds in proteins composed of 2…
Q: IUPAC name for the structure given. (DO NOT write "cis or trans") * H
A: Since this is a structure having a -COOH functional group and rest all is a CH backbone thus it…
Q: How many functional groups does the peptide MDFGRKCDE have that can be titrated? 6. 8. 7 O O O O
A: In organic molecules, the functional groups., which refer to the specific group of atoms presenting…
Q: Please Write the Structure Activity Relationship (SAR) of Losartan?
A: -Losartan is generally used to prevent heart attack or we can say that it's very useful in…
Q: What is the charge on histidine at neutral pH
A: Amino acids are compounds having carbon, hydrogen, oxygen, and nitrogen. They serve as monomers of…
Q: Draw the structure of the tetrapeptide 1. H,N - Lys - Ser-Asp- Ala - COOH Assign IUPAC names to each…
A: Protein or polypeptide is a sequence of amino acids in which the amino-terminal of one amino acid is…
Q: The pKa of the side-chain imidazole group of histidine is 6.0. What is the ratio of uncharged to…
A: A molecule is fully protonated at low pH, as the pH increases more than pKa of an ionizable…
Q: Classify the following nitrogenous bases into purines or pyrimidines.
A: Purines : Adenine and Guanine are purines . Pyrimidines : Thymine , Cytosine and Uracil are…
Q: Suppose you have a mixture of the following proteins protein A: pl = 3.5, mw = 35 kDa protein B: pl…
A: Cation exchange chromatography is defined as part of the ion-exchange chromatography. It is used to…
Q: (a) What is the net charge at neutral pH of a tripeptide containing only alanine? (b) How does the…
A: Alanine is an alpha-amino acid that is used in the biosynthesis of proteins. It contains an amine…
Q: Describe the concept of isoelectric point and calculate the PI for isoleucine?
A: Isoelectric point is the pH value at which the charge on an amino acid is zero.
Q: Consult Table 18.3 and draw alanine. Label the functional groups and give the three-letter…
A: Amino acids are the building blocks of proteins which contain amino group (-NH2 ) , carboxylic group…
Q: What are the charges of the following amino acids peptides at ph 14? 1. GLAVV 2. RRKKQ
A: Peptide chain is a short chain of amino acids joined by peptide/amide bonds (covalent bond). The…
Q: Draw the structure of each of the following tripeptides:(a) Lysine-phenylalanine-threonine(b)…
A: Peptides are formed from amino acids by losing a water molecule during the formation of the peptide…
Q: What constitutes the backbone of a nucleic acid?
A: Introduction: A nucleic acid is a biological large molecule composed of nucleotide chains. These…
Q: Five amino acids were subjected to normal phase chromatography, and the following Rf values were…
A: Retention factors are useful for the comparison of the results of chromatographic separation of one…
Q: What is the minimum number of polypeptide chains necessary for quaternary structure to exist?
A: The structural organization of protein was classified into four types: primary structure: formation…
Q: 1.2. Using DEAE-cellulose as ion exchange resin, indicate the starting and ending pH for the…
A: Negatively charged complex or protein can be separated by chromatography on positively charged…
Q: What is meant by the term polypeptide backbone?
A: A series of amino acids joined by peptide bonds form a polypeptide chain and each amino acid unit in…
Q: Following are two structural formulas for (S)-serine, one of the building blocks of proteins Is…
A: Amino acids Proteins are the polymers of nitrogenous compounds called amino acids. Each amino acid…
Q: What is the molecular basis for the observation that the overall charge on a protein becomes…
A: Hydrogen ions, are required in various chemical and biological processes. The available level of…
Q: Describe the principal biophysical and biochemical techniques used to study tertiary and quaternary…
A: The chain of amino acids where each amino acid is linked to others via a peptide bond is known as a…
Q: Please explain the following terms: Chirality Enantiomer Stereoisomer Diastereomer
A: The given terms are given by the molecules which have more than one chiral carbon present in them.…
Q: What is the Quaternary Structure?
A: The structural organisation of protein can be divided into four categories:i) Primary structureii)…
Q: After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by…
A: Protein purification is the process in which a protein or a number of proteins are separated or…
Q: Give the name and structure of at least two examples of each of the following: Heterocyclic…
A: Amino acids are the principal building blocks of the peptides and proteins in the living system.…
Q: What is the net charge at pH 7 on a peptide with the following sequence? -1…
A: In biochemistry, pH can be referred as the decimal logarithmic value of the reciprocal of H+ ions…
Q: Following are structural formulas for cytosine and thymine. Draw two additional tautomeric forms for…
A: The isomers which differ in the position and electrons and the carbon skeleton is same are said to…
Q: Based on molecular weights of purified (no beta-Me) and (beta-Me) sample, which are 140 kDa and 72…
A: Protein molecules are known to exhibit different conformational structures out of them the…
Q: The pH of the amino acid shown below is:
A: For an amino acid, the isoelectric point pH is calculated by taking the average of the two pKa…
Q: The net charge on this peptide at pH 9.5 is
A: A peptide is formed by number of amino acids joined with each other by peptide bond. Amino acids are…
Q: What is amphoterism? Show using chemical equations the amphoteric property of protein.
A: Proteins are one of the major biomolecules. It is made up of building blocks called amino acids.…
Step by step
Solved in 4 steps with 5 images
- The PI of protein P is 7.3. One can purify protein P by: Anion-exchange chromatography at pH 2.0 Anion-exchange chromatography at pH 7.3 Anion-exchange chromatography at pH 9.0 Anion-exchange chromatography at pH 4.3An ion-exchange chromatographic separation is performed using a diethyl-aminoethyl- (DEAE)-sepharose column to separate proteins in a mixture. The mixture contains Protein A (pl=6.0), B (pl35.0), C (pl=7.5), D (pl =1), and E (pl=4.0). The protein mixture is prepared in a buffer solution pH =5. When the protein mixture is loaded onto the column, and the column is washed with a buffer solution pH 5, which protein(s) will be captured by DEAE-sepharose in the column? O Protein B because it is predominantly in net negative charge form. O Proteins D and E because they have predominately net negative charge in pH 5 solution O Proteins A, C, D and E because they have charges O Proteins A and C because both both predominantly have net positive charges O Proteins Band E because both predominantly have net positive chargesSome characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 25,000 4.5 Yes 2 77,500 10.8 No 3 75,000 4.9 No a) Could gel filtration chromatography be used to separate a mixture containing Protein 1 and 2? Clearly explain why or why not. If it can be used, which protein would elute last (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins 1 and 2 be monitored at 280nm and 400nm (clearly explain)? b) Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by gel filtration? Why? c) Which 2 proteins listed in the table above could be separated by gel filtration chromatography but NOT by ion exchange chromatography? Why?
- A two-dimensional gel electrophoresis of a protein preparation revealed the presence of five monomeric proteins with the following molecular weights and Isoelectric points: | (10 kDa, pl = 5.6), II (25 kDa, pl = 7.7), III (55 kDa, pl = 5.6), IV (150 kDa, pl = 9.1), V (200 kDa, pl = 8.2). Using native chromatographic conditions which preserve enzymatic activity, what would be the predicted elution order for the five proteins on a gel filtration chromatography column: O1, II, II, IV, V O II, III, I, IV and V OV, IV, III, II, I O IV, V, II, III and I I and III, II, V, IVIn a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.Consider the titration of 30.0 mL of 0.0700 M HONH2 (a weak base; Kb = 1.10e-08) with 0.100 M HI. Calculate the pH after the following volumes of titrant have been added: (a) 0.0 mLpH = (b) 5.3 mLpH = (c) 10.5 mLpH = (d) 15.8 mLpH = (e) 21.0 mLpH = (f) 27.3 mLpH =
- Consider the equilibrium of arginine below: NH₂ NH₂ H₂N: NH OH H₂N- pKa=2.17 NH3 NH H₂NE pKa2=9.04 NH3 03 NH₂ NH HN: pka 12.48 NH₂ I II III If the pH of arginine solution is 8.08, what would be the major form of arginine? NH₂ NH 00 IV NH₂Refer to the following titration curve below: 13 12 11 10 9 7 6 5 4 3 4 6 8 10 12 14 16 18 20 22 24 26 28 30 Volume of Titrant / mL - Unknown Acid 0.10 mol/L - titrant = NaOH 0.1 mol/L At ph 10.0, which form of histidine is most abundant? His2+ His- His° His+You are given an equimolar (0.10 mM) mixture of Ubiquitin protein that is free/pure of any other macromolecules (e.g. nucleic acids) in a pH 7.0 phosphate buffer How can you purify Ubiquitin using Ion-Exchange chromatography (IEC)? Propose a plan using steps to purify this protein. Basic rules: Affinity chromatography (e.g. His Tag purification) is not an allowed step because these proteins are in their native state (i.e. – do not have a polyhistidine tag). Also, you are not allowed to rely solely on the color of certain proteins (e.g. cytochrome C and GFP) in your characterization/proposal. You are allowed to buffer exchange (i.e. – switch buffers) but try to keep your pH’s in a reasonable range (5.5 – 8.5) or you risk denaturing your protein. Assume proteins with the same charge (positive or negative) are not easily separated using IEC. Assume all proteins can be resolved/visualized on an SDS-PAGE gel. Ubiquitin Molecular weight (8663.02); pI (6.56); ε (M-1 cm-1) ignoring C’s…
- Using the generic structure shown, indicate what the substituents are for the structure of finerenone (R1, R2, R3, for Ar indicate R6, R8, R9, R10, for D indicate R4). R1 R2 R3 = For Ar: R6 R8 = R9 = R10 = For D: R4= Finerenone: H₂N HC Generic formula: H₂N 230 R+ 'R'. R$ ofWhen separated on a polyacrylamide gel, the procedure is abbreviated as SDS-PAGE (Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis). The technique is a standard means for separating proteins according to their molecular weight. The gels are neutral, hydrophilic, three-dimensional networks of long hydrocarbons cross-linked by methylene groups. (Give the main two compounds responsible for the formation of the gels)Draw the structures and indicate the net charge of the following amino acids for each pH value. Encircle the structure of the zwitterion and calculate for the pI. 1. Tyr (at pH: 1.5, 7.0, 9.5, and 11.0)2. Ser (at pH: 1.5, 7.0, and 9.5)