The first step in the procedure asks you to prepare five dilutions of the protein standard (BSA) in the range of 0.2 to 1.0 mg/ml. For each concentration, a volume of 1.0 mL should be prepared. Describe how you will prepare these standards using a stock solution of BSA that is 2.0 mg/ml.

Q: Explain which amino acids are acidic, which are basic, and which are neutral. Use theisoelectric…

A: Amino acids: At isoelectric point, proteins are neutral.

Q: The amino acid alanine is a solid at room temperature and has a melting point of 315 °C, while…

A: Reason to explain the existence of solid form of alanine but liquid form of pyruvic acid at room…

Q: Write the structure for the protein Pro-Asn-Tyr-Cys at pH 7.0.

A: Amino acid: An amino acid is an organic molecule and it consists of amine group (NH2), acidic…

Q: what is the concentration of the unknown protein in nanometers? use the information below! protein…

A:

Q: What additional single piece of information do you need in order to determine how much AP is being…

A: Answer: option c

Q: Select the correct statements about the isoelectric point of a protein. a. the charge on the…

A: Isoelectric point is the pH at which an amino acid or protein structure exist in its neutral form…

Q: Describe the tertiary and quaternarystructure of a protein.

A: Proteins are made up of long chains of amino acids. These amino acids are known as the monomers of…

Q: a. Explain why the presence of certain proteins in body fluids such as urine or blood can indicate…

A: a. A group of amino acids combining together to form various molecules are called proteins. They are…

Q: Calculate the number of millimoles(mmol)in 500 mg of each of the following amino acids: alanine…

A: The relation between mass, molar mass and mole is given by : Mole = mass/molar mass

Q: 2.) An unknown amino acid was subjected to paper chromatography with five amino acid standards in…

A: Paper chromatography -  Is partition in which the various components  get distributed between…

Q: M anserine buffered solution, pH 7.20. Answer the below questions: Volume of stock solution needed =…

A: Given 0.200 M solution of anserine at its isoelectric point  0.200 M HCl, 0.200 M NaOH and distilled…

Q: Which of the following statements describes the amino acid presented below? OH CH2 O H3Ñ–CH-C-0 This…

A: The R group in an amino acid is its side chain. This side group make it hydrophilic if it can make…

Q: description for the term rancidity of oils two causes of rancidity of oils acid value of oils

A: The oxidation reaction is a kind of chemical reaction in which the substance gets oxidized either by…

Q: Net charge and isoelectric point of an amino acid with an ionizable side group.Consider the net…

A: Hey since you have posted a question with multiple sub-parts, we will solve first three sub-parts…

Q: Draw the tripeptide Alanine-Cysteine-Serine (R1 = CH3, R2 = CH2SH, R3 = CH2OH) under the following…

A: The structure of tripeptide Alanine-Cysteine -Serine is shown in the below steps at different pH, At…

Q: .) Explain the observed pH of the solutions of the amino acids glutamic acid and lysine.

A: Since you have posted multiple questions as per guidelines we can answer only one per session . If…

Q: What other factors can also affect the solubility of protein?

A: The solubility of proteins can be affected by following factors ; 1. pH of a protein : The…

Q: How many mls of an aminophyllin solution (500mg/20ml) is needed to prepare 425mg aminophyllin in…

A:

Q: 7. Explain why it is easier to digest cooked fish than sushi (raw fish.) Discuss the differences in…

A: It is easier to digest cooked fish compared to raw fish, because the process of cooking the fish…

Q: Consider a buffered solution with a pH of 11 that contains tyrosine as a free amino acid. W the net…

A:

Q: Which of the following statements are correct about the process of protein structure determination…

A: Proteins are the building blocks of life which are composed of amino acids and these are arranged…

Q: Describe the pH range of acceptable buffering behavior for the amino acids alanine, histidine,…

A: The pH range of amino acids alanine, histidine, aspartic acid, and lysine is to be described. Amino…

Q: The pH of a solution determines the form of an amino acid. Determine which condition corresponds to…

A:

Q: Write general equations showing the ionization of a protein in acid medium and in basic medium.…

A: Structure of protein : NH2 -R-COOH NH2 = Basic groupCOOH = Acidic groupR= Alkyl or Aryl group    1.…

Q: The image above depicts protein tertiary structure. What type of tertiary structure is represented…

A: Given: Tertiary structure of protein  To find: Type of bonding at letter b  Solution: Tertiary…

Q: A protein has minimum solubility dissolved in a solution of 2.0 mL of water, 7.0 mL of 0.2 M sodium…

A: Given: The concentration of sodium acetate = 0.2 M The concentration of acetic acid = 0.5 M…

Q: Describe two examples of protein folding patterns and identify what level of protein structure they…

A: 1. Two examples of protein folding pattern is tertiary structure and quartenary structure. Tertiary…

Q: Draw a representative amino acid, labelling the side group as R and identifying the amino and…

A: Amino acid : an amino acid is an organic molecule that is made up of a basic amino group (−NH2)  an…

Q: "A protein has a pI point which can be used to separate proteins using ion exchange. If you have an…

A: PI value or isoelectric point of a protein is its pH at which it carries no net electrical charge…

Q: 9. For the two amino acids below determine if each of them would be either on the inside or the…

A: In the tertiary structure of protein hydrophobic moiety resides inside the cell interior and…

Q: Why is it important/useful to prepare active ingredients that contain an amino group as ammonium…

A: Solubility of Ammonium Salts When an amine is added to a solution of a strong acid, such as…

Q: A solution of the amino acid Lysine is at pH 13. What will be the overall charge, the charge on the…

A:

Q: The amino acid phenylalanine can be made in the laboratory. Choose the correct reagents needed to…

A:

Q: Solve this

A: Proteins are formed by condensation reaction of amino acid in which by product such as water is…

Q: Does the titrated amino acids appear to be acidic, basic, or neutral amino acids? Please explain…

A: Amino acid is the acid contains acid group and and the amine group . Ehen there is more than one…

Q: I only need the column: NAME OF THE TEST and (+) RESULT

A:

Q: Propose a step-by-step procedure to separate the amino acids glycine and tyrosine mixture using Thin…

A: Given : Glycine and tyrosine amino acids  To Find : Procedure for separating the two amino acid…

Q: For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which…

A: Here, we have to estimate the ratio of the concentration of the neutral amino acid species to the…

Q: For aspartic and glutamic acids, the isoelectric point occurs at a pH where the net charge on the…

A:

Q: (a) Describe in detail how you will determine the primary structure of protein. You have been given…

A: (a) Primary structure of protein The primary structure of a protein is generally referred to the…

Q: a. Tyrosine b. Alanine c. Leucine d. Asparagine 5. Draw a picture showing the details of the…

A:

Q: Describe three effects of pH on ionization of a weak acid or base that impact biological stability…

A: The three effects of pH on ionization of a weak acid or base that impact biological stability of a…

Q: The secondary structure of a protein is the Multiple Choice Ospecific order of amino acids in the…

A: Secondary structure refers to regular, recurring arrangements in space of adjacent amino acid…

Q: how could the formulation scientist prevent aggregation of a protein drug?

A: Protein aggregation: A biological phenomenon in which intrinsically misfolded proteins or disordered…

Q: If you take 0.280 g of an unknown amino acid, dissolved it in 100 mL of H2O (added HCl), then…

A: Given that -  Mass of unknown amino acid = 0.280 g  Total Volume of This compound  = 100 mL  Volume…

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: Almost all proteins are composed from a set of about _____ amino acids. a. 4 b. 10 c. 20 d. 50

A: Hello. Since you have posted multiple questions and not specified which question needs to be solved,…

Applications of Molecular Spectroscopy

When light sources pass through the diffraction grating then light splits into different wavelengths. The light source produces two types of patterns that are shown as destructive and non-destructive. The light source is in the form of quanta that is quantitation.