Peptides & X-ray/NMR Methods Q4.2- Describe one advantage and one disadvantage of trying to solve molecular protein structures by 1) X-ray crystallography and by 2) Nuclear Magnetic Resonance (NMR) spectroscopy.
Q: Why do we use methanol into the solid phase extraction cartridge to extract the acidic fractions and…
A: The acidic fractions in drugs contains groups such as -COOH. The basic fractions in drugs contains…
Q: In Biochemistry，What is the main characteristic of peptide bond？what does it means by partial double…
A: Introduction Amino acids are the building blocks of proteins. Proteins is the most abundant…
Q: Figure 4.16 - Structure of the Heme Group N H Pyrrole OOC H₂C H₂C H₂C H₂CC HC C-C H = C HgC C NH N 1…
A: These images correspond to the structure or components of heme, an integral part of hemoglobin…
Q: please check if I get prolin‘s charge correctly
A: Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…
Q: 1. Below is a free energy graph for the chemical reaction A + B àD.
A: Free energy is used to determine the state of the any reaction, i.e. how can systems change and also…
Q: Of the components in the hydrogels beads, which is the protein we are interested in measuring?
A: Hydrogel beads are cross-linked mesh of hydrophilic polymers which is composed of spherical shaped…
Q: HO
A: Fatty acids must first enter the cell through the cell membrane, then bind to coenzyme A (CoA),…
Q: In dialysis protein purification technique, the mebrane tubing needs to be pre-wet. Why? What would…
A: The source of protein is called crude extract. It consists of protein(s) of interest as well as…
Q: Draw the arrow-pushing mechanism
A: The transfer of amino acid residue from aminoacyl-tRNA to peptidyl tRNA is an important reaction in…
Q: An allosterically regulated enzyme in the R state is unable to bind substrate at the active site.…
A: Allosteric site : It is a place or site on an enzyme where the molecule which is not a substrate can…
Q: Vancomycin is a very potent antibiotic use for several diseases such as infective endocarditis,…
A: Vancomycin is a unique glycopeptide that is structurally unrelated to most common antibiotics. This…
Q: What would you predict about the ratio of hydrophilic to hydro- phobic amino acid residues in a…
A: Before getting into the calculations, we have to assume that our globular protein have a spherical…
Q: Biolink 'Drugs and their Conformations' (a) Which drug is more likely to produce multiple…
A: A drug with confirmational flexibility is a good drug as it will produce more physiological effect.…
Q: which amino acids have basic side chain and which amino acids have acidic side chain？？what does it…
A: Amino acids are the building blocks of proteins which are composed of amino group (NH3+), carboxyl…
Q: Compare and contrast fermentation, aerobic respiration, and anaerobic respiration in BACTERIA. Be…
A: Fermentation of is a partial oxidation or reduction of sugars to other organic compounds.…
Q: 6) Proteins can be modified by phosphorylation, which adds a phosphate group to the hydroxyl group…
A: Protein modification - Major types of proteins modifications are phosphorylation, acetylation and…
Q: Describe the structural basis for the cooperative (allosteric) binding of O2 by hemoglobin but not…
A: Both hemoglobin and myoglobin are oxygen transport proteins. Both of them are complex proteins…
Q: Which of the following is/are (a) ketopentose? A. threose B. xylulose C. arabinose D. mannose
A:
Q: 1. What is mucic acid? 2. What is the principle involved in mucic acid test?
A: When nitric acid oxidizes both the C1 aldehyde and the C6 primary alcohol of an aldose, a saccharic…
Q: 4. Describe aldonic acids, uronic acids, alditols, deoxy sugars, and amino sugars.
A: Modified monosaccharides are called sugar derivatives. Monosaccharide molecules that have undergone…
Q: What would be the biuret test result if the specimens tested are alanine and casein? What group in…
A: Note: Hi! Thank you for the question. We are authorized to answer one question at a time. Since you…
Q: Consider the following: NO3 → NH4* The balanced half-reaction is A. B. C. D. NO₂¯ +10H* +9e¯ → NH4*…
A: Oxidation is a process by which an atom loses electrons while reduction is a process of gain of…
Q: The graph is an example of the rate of product production by an enzyme when the substrate is in…
A: An enzyme has substrate binding site. When substrate binds to that site, the reaction takes place.…
Q: Gluconeogenesis Q3.4 - Considering that gluconeogenesis requires a net input of 4 ATP equivalents…
A: Gluconeogenesis is the process of formation of glucose from non-carbohydrate sources such as…
Q: Using an arrow, draw the site of cleavage for the following peptide that is reacted by: Pepsin…
A: Any peptide or protein can be cleaved by numerous protein digestive enzymes such as pepsin, trypsin,…
Q: A mixture of the following amino acids (glu, leu, val, arg, ser, phe) was obtained upon complete…
A: The following amino acids (glu, leu, val, arg, ser, phe) were obtained from complete hydrolysis of a…
Q: Proteins tracked by fluorescence recovery after photobleaching (FRAP) showed that they are ALL…
A: Introduction: Fluorescent markers get excited at a particular wavelength of light and undergo…
Q: In an antibody, the heavy chain polypeptides are attached to the light chain polypeptides through…
A: Since antibody is a tetrameric structure consisting of 2 light chains and heavy chains so it is a…
Q: Nomenclature of vitamins (empirical, biochemical, medical).
A: Vitamins are organic nutrients which can not be synthesized in the body, hence, need to be supplied…
Q: A cell in a hypertonic solution swells because of a net loss of water by osmosis. True False
A: A hypertonic solution is a solution that contains high solute concentration. Osmosis is the…
Q: 1) How many different forms of D-monosaccharide are present at equilibrium in an aqueous solution?…
A: “Since you have asked multiple questions, we will solve the first question for you. If you want any…
Q: After heating albumin at a high temperature, does it still biologically active? Explain why.
A: Proteins structure and function are affected by several factors such as temperature, pH, detergents,…
Q: Select the answer with an INCORRECT statement about the hydrophobic effect It is important for…
A: Hydrophobic effect is the tendency of non polar molecules to interact with each other in polar…
Q: What is the difference between cellobiose & cellulose? A. Cellulose is a starch molecule,…
A: Carbohydrates are linked together via glycosidic bond in order to produce different types of…
Q: Draw the Catabolism of triacylglycerols- beta-oxidation Pathway and identify different types of…
A: Fatty acids are transported into the cell. The enzyme fatty acyl-CoA synthase(FACS) adds a CoA group…
Q: Using drawn graphs or image, xan you explain the factors like pH, temperature, substrate…
A: Enzymes - Enzymes are giant protein molecules that act as biological catalysts. Like other chemical…
Q: Predict the amino acid sequence based on the conditions below. Use the one-letter abbreviation of…
A: Amino acids are building block of polypeptide chain. its alpha carbon contains carboxyl group, amine…
Q: A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a equilibrium constant (Kd) value…
A: ∆Cp is the heat capacity at constant pressure. ∆S is change in entropy, degree of randomness. At…
Q: Ceruloplasmin is a blue-colored monomeric oxidase found in mamma- lian blood plasma. It contains…
A: Ceruloplasmin is a copper containing globulin which helps in the transport of copper in the…
Q: Comparing the active site geometries of chymotrypsin and subtilisin enzymes under the hypothesis…
A: Chymotrypsin : it is a very powerful proteolytic(protein breakdown enzyme) which is being secreted…
Q: A decapeptide composed of ser, ala, IIe. his, trp, phe was treated with 1-flouro-…
A: Protein sequencing is a process of determining the sequence of amino acids in a protein. There 2…
Q: Explain why condensed milk is not advisable to infants. 2. Enumerate the different kinds of milk.
A: Introduction Milk is the the primary source of nutrition for young mammals. It is a white colour…
Q: Question 6 At pH 9.0, which of the peptides listed in Question #4 would bind tightest to a…
A: Hydrophobic interaction chromatography (HIC) separates molecules based on their hydrophobicity. HIC…
Q: What does glutamic acid do to the membrane potentials of: Neurons - Muscles -
A: Glutamic Acid : It is an α amino acid which is used by all living beings & organisms in the…
Q: 3. The general properties of amino acids: a) formation of zwitterion; b) the acid-base properties…
A: All living organisms employ amino acids as building blocks for proteins. Twenty different amino…
Q: 5. Specific properties of amino acids in the organism: a) deamination; b) transamination; c)…
A: Amino acids are the building blocks of proteins, its alpha carbon contains carboxyl group, amine…
Q: In bacteria, one of the main functions of pilli is A. Buoyancy B. Conjugation (genetic exchange) C.…
A: Based on nutritional mode, bacteria can be classified as autotrophic bacteria (those that can…
Q: in the presence of a noncompetitive inhibitor 24) Relation between Reaction Velocity and Substrate…
A:
Q: 3-1. For each of the given amino acids, write the equilib- rium reactions that would apply at a pH…
A: The proteins re composed of amino acids having an alpha amino, alpha carboxyl and a side chain. The…
Q: What is the pH at which the tripeptide Gly-Ala-Gly has a net charge of 0?
A: The net charge of a peptide is calculated by adding the charges of amino and carboxy terminal of the…
384
Peptides & X-ray/NMR Methods
Q4.2- Describe one advantage and one disadvantage of trying to solve molecular protein structures by 1) X-ray crystallography and by 2) Nuclear Magnetic Resonance (NMR) spectroscopy.
Step by step
Solved in 2 steps
- MATHEMATICAL Calculate the isoelectric point of each of the following amino acids: glutamic acid, serine, histidine, lysine, tyro- sine, and arginine.[Ten - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly Questions; Thomas was purifying an enzyme from a homogenate of muscle cells. He went through seven steps of purification and found that the enzyme activity was the same as the homogenate value. On the eighth step, when the protein washighly pure, the enzyme activity rose to five times that of the homogenate value. Can you suggest a possible reason? A. the homogenate assay was wrong B. step eight has co-purified an activator of the enzyme. C. the enzyme has an inhibitor present in the muscle cell homogenate D. the temperature at step eight was just right for the enzyme activity.Topic: ISOLATION AND CHARACTERIZATION OF PROTEINS 1. Which amino acids contains the following:a. Sulfur/sulfhydryl groupb. Aromatic groupc. Imidazole ringd. Guanidine groupe. Indole ring2. Classify the following proteins to their biological functions (casein, albumin, gluten, andmyoglobin) 3. Which level of protein structure organization are lost hydrolysis and denaturation?4. What is the Beer-Lambert’s Law? Why is it relevant to the quantitative analysis of proteins?
- Given: Cryo-EM structure of PCoV_GX spike glycoprotein 1. What can you tell me about the identity of the protein? 2. What is the importance of this protein?GABA (B) Need help answering these questions about the GABA(B) protein. What class (globular, fibrous, membrane) protein is the protein Identify the organism (or organisms that have this protein) Identify the cellular location of this protein Describe the function Find the primary structure (list it on a slide) Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein) Find a picture of the tertiary structure (which should also show secondary structure) Does the protein have a quaternary structure, if so what is it?Subject: Biochemistry, chemistry, polyacrylamide gel electrophoresis Differentiate native PAGE and SDS-PAGE in terms of the relative molecular weight of protein bands obtained. Explain your answer.
- identification What are the building blocks of proteins? What type of hydrolysis will cleave a protein at a peptide bond? What qualitative test is used to detect peptide bonds? What is the positive result for the answer in no. 6? Proline will produce what result in the ninhydrin test? Which component of the Hopkins-Cole reagent will react with tryptophan? The reaction in Fohl’s test will cause the formation of what compound? What type of reaction happens in Pauly’s test?2. . 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. Calculate the overall charge (pH 7) on the following three polypeptides and answer the (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 (g) Which of the three peptides would migrate the furthest away from the anode in isoelectric fo- cusing (h) Which of the peptides would migrate the closest to the cathode in isoelectric focusing?…10-20. Find the pH and the concentration of each species of lysine in a solution of 0.010 0 M lysine ·HCI, lysine monohydrochloride. The notation "lysine ·HCl" refers to a neutral lysine molecule that has taken on one extra proton by addition of one mole of HCl. A more meaningful notation shows the salt (lysineH†)(Cl ) formed in the reaction.
- E. PROTEIN PRIMARY STRUCTURE ELUCIDATION. 1. Determine the primary structure of the protein described below. Write the final sequence using the corresponding three-letter code for each amino acid. Example: M-F-Y-R should be written as Met-Phe-Tyr-Arg Treatment with cyanogen bromide and sequencing yields the following peptide fragments: o D-M o R-A-Y-G-N o L-F-M Chymotrypsin digestion and sequencing yields the following peptide fragments: o G-N D-M-L-F o M-R-A-Y o o3 Acra Alrich TOI NOF 200 250 300 350 Wavelength (nm) UV/Vis spectrum of four brands of polysorbate 80, a common detergent used in protein purification. From Wuelfin, et al., "Polysorbate 80 UV/vis spectral and chromatographic characteristics-defining boundary conditions for use of the surfactant in dissolution analysis." 3. While the binding of Coomassie blue to proteins can lead to accurate measurements of protein concentration, there are situations where the absorbance values could be misleading. For example, detergents are often used in the purification of proteins. Certain detergents mixed in with the dye could lead to incorrect determinations of protein concentration. Take a look at the spectrum of the detergent polysorbate 80, above. If you had used this detergent to purify the protein in part c above, would you expect it to interfere with your concentration calculations? Why or why not? Absorbance (AU)GABA (B) protein Need help answering questions about the GABA(B) protein. What is the primary structure Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein)What is the tertiary structure (which should also show secondary structure)Does the protein have a quaternary structure, if so what is it?
