draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 put the name of each part and the charge pls then compute for the isoelectric point please show complete solution KRINPLA

draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 put the name of each part and the charge pls then compute for the isoelectric point please show complete solution KRINPLA

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: Sketch the MO diagram for 1,3 budadiene. Determine the net bonding interactions for ¥2 and ¥3. How…

A: The mathematical function that illustrates the wave-like function and location of an electron in a…

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

A: Given, Data for glycine pH pKa-COOH =2.3 pKa-NH3 = 9.6 CN ∆Eq 0 0 +1 +1 0 2.3 -0.5 +1 +0.5…

Q: Using skeletal structures, draw the structure of a simple triacylglyceride containing 1…

A: A triglyceride is an ester derived from glycerol and three fatty acids.

Q: Table 4- Determination of the optimum pH of catechol oxidase enzyme Potato extract (mL) Tube # 2d 3d…

A: Enzymes are biocatalyst that perform specific biochemical reaction in living organisms. They are…

Q: Determine the net charge (to the nearest integer) on the following peptide at pH5 AND pH 12.…

Q: Indicate which of the amino acid residues in the following peptide sequence contains a group that…

A: Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…

Q: draw the primary structure of the polypeptide at physiological pH range of 7/35-7/45 using…

A: Polypeptide chains are composed of amino acids bonded to each other via peptide bonds. The N and C…

Q: 3.4. A protein solution is prepared by dissolving 800 µg of protein in 200 µL of water. A 150 µL…

A: The four types of biological macromolecules are nucleic acids, proteins, lipids and carbohydrates.…

Q: The tripeptide +H3N-Leu-His-Glu-COO- has pKa values of 2.2, 3.6, 6.0 and 9.1. The isoelectric…

A: Isoelectric point (pI) is the pH at which there is no net charge on the molecule. For a amino acid,…

Q: Draw the chemical structure of the tripeptide CYS-LYS-ALA at pH 4.5. (show all atoms that are part…

A: Amino acids bind to each other through a peptide bond. This bond is formed between the carboxyl…

Q: What is the isoelectric point of HPY? 5.70 6.15 6.875 7.60 8.05

A: Isoelectric point (pI) is the pH at which a species (here a tripeptide) have 0 charge (i.e.…

Q: You want to make 94 µL of the diluted Cell-Free extract for estimation of total protein. To do this,…

A: A ratio of 1:25 means add 1 part of product to 25 parts of water. Dilution factor does not gives…

Q: draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 using…

A: The primary structure of the polypeptide at physiological pH range of 7.35-7.45 using condensed…

Q: 1. Draw the structure of triacylglycerol that contains oleic, linolenic, palmitic acids. Is it oil…

A: Carbohydrates are the polyhydroxy aldehydes and ketones with the general formula Cx(H2O)y. They are…

Q: Sketch out the titration curve below and the structure(s) of the major ionic form(s) of glutamic…

A: Amino Acids: Amino acids are organic composites that serve as the abecedarian structure blocks of…

Q: During movement, muscle cells require large amounts of ATP to fuel their contractile apparatus.…

A: Cell is the smallest structural and, functional unit of life. It is simple machinery that houses all…

Q: Match lipid descriptions in column A with the phospholipid type in column B ✓ H is attached to the…

A: Membrane is composed of phospholipids whose structure has polar head group & non-polar tails.…

Q: Analyze each item carefully and write your complete solution. Cysteine is an important amino acid…

A: Titration curve: Titration curves are created when successive additions of acid or alkali cause the…

Q: Size Size Crude Anion Cation 2) Exclusion Exclusion Lysate Exchange Exchange 1 2 Total Protein…

A: Enzymes are vital to life and constitute one of the human body's most significant protein groups. A…

Q: Theoretically, the pI of myoglobin is 7.2. In phosphate buffer pH 6.0, what is the overall charge of…

A: Proteins are composed of twenty standard amino acids attached together via peptide bonds. Myoglobin…

Q: What is the molecular weight of a linear polysaccharide consisting of 7 galactose monomers and 1…

A: Glucose and galactose are monosaccharides that are also referred to as simple sugars. They represent…

Q: Determine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at: a. pH 1.0 b. pH…

A: The estimated charge on the given Lys-Ala-His-Asp-Ser peptide is +3.At low pH, the amino acid is…

Q: What is the dissociation equilibrium constant of a protein if the concentration of free ligand is…

A: Consider the following reaction: P + L ⇌k2k1 PL where P is the protein, L is the ligand and k1 and…

Q: draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 put the name of…

A: Proteins are unbranched polymers constructed from 20 standard α-amino acids. They have four levels…

Q: 80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is…

A: Proteins are unbranched polymers constructed from 20 standard α-amino acids. They have four levels…

Q: You are trying to separate study Fibrinogen variants with a pl approximately 5.8. Which ion exchange…

A: The method comprises a blood separating step of taking bovine blood and adding an ... separation…

Q: Ala-Phe-Pro-Cys-Clu-Arg-Arg-Pro-His-Gly-Lys-Clu Calculate the net charge on the polypeptide at a.…

A: Note: There is no amino acid with a three-letter code as Clu. The charge calculation will be carried…

Q: Draw the Ala-Ser-Leu-Asp polypeptide (perspective formula) showing the fully extended backbone…

A: Proteins are folded peptides. Peptides are polymers made up of amino acid residues linked via a…

Q: Some phospholipid species can be phosphorylated beyond the phosphate attached to the #3carbon.…

A: The basic structure of a phospholipid consists of two fatty acid chains attached to the C-1 and C-2…

Q: Part A Consider the structure of glucose: H-C=O Submit Request Answer -OH H- HO- -H H- H -OH -OH OH…

A: Glucose, a fundamental building block of carbohydrates, is a simple sugar molecule with a profound…

Q: A sample mixture consists of three proteins with the following properties: MW (kDa) 200 Amino acid…

A: As per our guidelines, we are supposed to answer only three sub-parts. Kindly repost the question…

Q: draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 and put each…

A: The polypeptide of a protein is composed of different amino acids that are joined together through…

Q: Draw the condensed structural formula of a gycerophospholipid trat contains two stearic acids and a…

A: Definition of condensed structure - The system for writing organic compounds in a single line is…

Q: 0.03 The uv spectrum of a protein solution shows A280 nm = 0.43 and A260 nm = What is the…

A: When working with proteins, one necessary part of any good assay is accurately determining how much…

Q: draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 using…

A: A polypeptide is an amino acid chain molecule where the carboxyl group of one amino acid is linked…

Q: You are given 0.5 M solution of the amino acid Arginine. pK1 (α-carboxyl group) = 2.17 pK2 (α- amino…

A: In biochemistry, pH can be referred as the decimal logarithmic value of the reciprocal of H+ ions…

Q: - Draw the structure of the pentapeptide Gln-Trp-His-Glu-Tyr that would predominate in aqueous…

A: Amino acids are biomolecules that are made up of two functional groups, these are an amino group and…

Q: Protein Isoelectric pH Molecular weight (kDa) Ovalbumin 4.6 45 Insulin 5.4 5.7 Fibrinogen 5.8 340…

A: The isoelectric point of a protein is the pH at which the net charge of the protein is zero. At this…

Q: Discuss the primary structure and/or unique amino acid composition, three-dimensional structure…

A: A fibrous protein is a protein with a lengthened shape. Sinewy/fibrous proteins offer underlying…

Q: draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45 put the name of…

A: Polypeptides are composed of twenty standard amino acids. These twenty standard amino acids differ…

Question

draw the primary structure of the polypeptide at physiological pH range of 7.35-7.45
put the name of each part and the charge pls
then compute for the isoelectric point please show complete solution

KRINPLA

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

VIEW

Step 2

VIEW

Step by step

Solved in 2 steps with 2 images

SEE SOLUTION Check out a sample Q&A here

Similar questions

80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.
the enzyme LCK catalyzes the hydrolysis of the peptide KEY in 5.0 mM phosphate buffer at pH 7.0. The enzyme is known to obey Michaelis-Menten Kinetics. Under the conditions of this experiment: Vmax= 10 mmol/min/mg Km (KEY) = 0.20 mM Draw the complete structure of the tripeptide KEY and calculate its molecular weight Sketch the titration curve of the above tripeptide and label it.Determine the net charge of the peptide at each pk value Calculate the PI pf the peptide and draw the structure of the peptide at the isoelectric point.
Given the titration curve of the hypothetical polyprotic acid X at 0.100 M concentration (pKa1=4.0, pKa2=8.0, pKa3=12.0) titrated with 0.600 M NaOH, identify the pH at point C, H, E, and M.
Determine the class of lipid (see attached image for choices) shown by the following structures and whether if it is saponifiable or non-saponifiable.
6-73 In each case, tell which side (if either) rises and why. The solvent is water. A A Osmotic membrane (a) 1% glucose (b) 0.1 M glucose (c) 1 M NaCl (d) 1 M NaCl (e) 3% NaCl (f) 1 M NaBr (B) B 5% glucose 0.5 M glucose 1 M glucose 1 M K₂SO4 3% KC1 1 M KC1
At pH 7, tryptophan crosses a lipid bilayer at about onethousandththe rate of indole, a closely related compound: Suggest an explanation for this observation.
Major functional groups present and expected wavenumbers of the peaks: Attach IR spectrum of the compound and list wavenumbers of signals/peaks observed in the spectrum: Discussion
the overall, net ionic charge on this peptide at pH = 7 would be: Cys - Ala - Glu-Arg - Met - Ser
A protein has a dissociation equilibrium constant equal to 4.0um. What is the concentration of free ligand when the fraction of bound sites is 0.7
Titration curve of an unknown amino acid The graph below shows a curve, which was obtained following titration of an unknown amino acid. Include a suitable descriptive title stating the identity of the unknown amino acid Use rectangles to precisely outline the regions in the graph where ionisable groups show buffering activity (base/acid ratio 1:10 to base/acid ratio 10:1); clearly associate the name of the ionisable group with the buffering regions; indicate within the graph all observable titration mid-points and all observable titration end-points and indicate estimates of the pKa of the three functional groups (do not provide pka values from the literature, you need to read the pka from the titration curve provided). Note that it is not possible to estimate the pka with more than one decimal precision due to limited resolution of the shown graph.
To prepare a gel sample, you want to load 50 ng total of protein/well. You have added 200 μL of protein in 800 µL reagent and measured your sample by Bradford A595 to be 0.7 mg/mL - your dilution is unaccounted for at this point. Assuming a total final volume of 20 μL, what volume of protein sample, buffer and 4X SDS PAGE Loading Dye needs to be mixed to create a final sample of 50 ng protein in 20 μL?
Give detailed Solution with explanation needed (don't give Handwritten answer