1. In Part II of the Procedure, you were instructed to use your original mixture of phycocyanin and 0.10M sodium phosphate buffer as your reference solution because the buffer stabilizes the protein in its native (folded) form. Briefly explain how the buffer stabilizes the phycocyanin.

1. In Part II of the Procedure, you were instructed to use your original mixture of phycocyanin and 0.10M sodium phosphate buffer as your reference solution because the buffer stabilizes the protein in its native (folded) form. Briefly explain how the buffer stabilizes the phycocyanin.

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

See similar textbooks

Related questions

Q: You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino…

A: The mixture of amino can be separated by electrophoresis technique. This method is based on pH…

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

A: The pure (S)-alanine is an enantiomer. Enantiomers are optically active compounds. Thus, (S)-…

Q: 1) Proteins undergo a process called thermal denaturation. This is a process where the protein…

A: Spontaneity of a reaction means will the reaction proceed in forward reaction without any need of…

Q: Your task is to categorize and tabulate the 20 standard amino acids with the following columns:

A: Amino acid are the building block of protein which contain both acidic COOH and basic NH2 group

Q: 9. How do you know if a malenimide based reagent will conjugate to nitrogen or sulphur in an amino…

A: we can identify the malenimide based reagent as amino acids by looking at the following - amino…

Q: For this assignment I want you to look up some of the following compounds with their conjugate acid…

A: If the pH is greater than pKa then deprotonation occurs and it exists in deprotonation form. While…

Q: Answer the following problem and show your detailed solution and explanation. The tripeptide…

Q: Rank these basicities of the amine groups in these amino acids according to their expected pK,…

Q: Draw Tryptophan in a peptide bond. Explain all of the bonds using valence bond theory (VBT). Next,…

Q: DRAW THE CHEMICAL STRUCTURE OF THE FOLLOWING: 1) Methyl 5-methyl-6-oxohexanoate 2)…

A: The chemical structures has to be drawn.

Q: 8. The following proteins represent a wide range of molecular weights and isoelectric points. Mr is…

Q: 13. In the physiological pH range, the nitrogen in the imidazole ring can be easily…

A: The Bronsted acid is a substance that donates a proton(H+). The Bronsted base is a substance that…

Q: Identify the amino acids in the following tripeptide: HN-CH-C-NH-CH-C-NH-CH–C-O CH2 CH,OH…

A: Find the peptide linkage i.e. CONH linkage. Break the bond between Carbon and Nitrogen atom and thus…

Q: Draw the structure of the most abundant form of cysteine in solutions whose pH values are 1, 4, 6,…

A: The molecules found inside human body which have carboxylic and amine group containing monomer units…

Q: The first step in the catabolism of most amino acids is the removal of the nitrogen atom by transfer…

A: Organic reactions are those in which organic reactant react to form organic products.

Q: Lysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to…

A: Lysine- Structure is- Lysine consists of α-amino group ,α- carboxylic acid group also side chain…

Q: Number

A: We know that, Proteins chain of amino acids joins together to form protein. Proteins are found in…

Q: Consider the amino acid molecule shown below in a Fischer representation. Which of the following…

A: In D and L configuration, to represent optical activity of compound:D or Dextro configuration…

Q: Show how L-Serine can act as buffer when you add H3O+ or OH- ions Write equations to show this.

Q: Draw a titration curve for the following peptide and circle the region(s) where this peptide would…

Concept explainers

Coding Strand of DNA

When pointing to DNA transcription, the coding strand is found to be the DNA strand whose base sequence is indistinguishable from the base sequence of the RNA transcript developed. It is this strand that comprises the codons, while the non-coding strand comprises the anti-codons.

Nucleotide

Both DNA and RNA are composed of organic molecules known as nucleotides. Hence, nucleotides are known as the basic building blocks of nucleic acids. These substances play a role in various processes such as cell signalling, enzyme reactions, metabolism, and so on.

Structure of Cytosine

Cytosine is among the five primary nitrogenous bases of which DNA and RNA and are being used in storage and transportation of genetic makeup within a cell. Adenine, guanine, thymine as well as uracil are the remaining four nucleobases.

Question

Chemistry
Use the spaces provided for the answers and additional paper if necessury.
1. In Part II of the Procedure, you were instructed to use your original mixture of phycocyanin and
0.10M sodium phosphate buffer as your reference solution because the buffer stabilizes the protein in
its native (folded) form. Briefly explain how the buffer stabilizes the phycocyanin.

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 2 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, chemistry and related others by exploring similar questions and additional content below.

Similar questions

There are 20 common, naturally occurring amino acids from which all proteins are derived (as will be discussed in Chapter 25), although many other less common amino acids have been isolated from natural sources. Valine is one of the 20 common amino acids, and it was used as a starting material in the laboratory synthesis of an uncommon amino acid (Tetrahedron 1997, 53, 1151-1156). During one of the steps in the synthesis, compound 1 was treated with HBr under conditions that favor radical addition, giving stereoisomers 2 and 3. Draw the structures of 2 and 3, and describe their stereoisomeric relationship. H. LOCH3 HBr 2 + 3 hv H (S)-valine Modify the given copies of compound 1 to drawthe structures of 2 and 3. You can use the single bond tool to add/remove double bonds. CH2 CH2 H,C- H3C- -CH, -CH, Edit Drawing Describe the relationship of 2 and 3. O They are enantiomers. O They are superimposable. They are diastereomers. O They are constitutional isomers.
The structure of a triacylglycerol molecule can be described in terms of the fatty acyl groups that appear at each of the three positions along the glycerol backbone. Human milk contains a triacylglycerol with an oleoyl residue at position 1, a palmitoyl residue at position 2, and a linoleoyl residue at position 3. Draw the structure of this molecule, using the information in the table below. For example, an oleoyl residue is derived from oleic acid.
4 How does aqueous Silver nitrate, AGNO3, works against neonatal conjunctivitis (inflammation of the outer eye) due to neonatal bacterial infection? It hydrolyzes protein in bacteria to amino acids and inactivate it. O It denatures the protein bacteria and kills them. It mutates the genetic make-up of bacteria and transforms them to useful proteins. It oxidizes side chains of cysteine residues to cystine.
Show the detailed experimental procedures for the chemical synthesis of proteins with the α-ketoacid–hydroxylamine (KAHA ligation), using (S)-5-oxaproline (Opr) as a key building block.
The pka of ascorbic acid is 4.2 at 24C. At what pH is the ratio of the deprotonated form to the protonated form 10:1? Prove using the Henderson-Hasselback equation. How to resolve this.
1. What reaction is catalyzed by the enzyme carbonic anhydrase? Which metal ion serves as a cofactor for carbonic anhydrase? Explain how this metal ion is able to assist in catalyzing the reaction. 2. In relation to enzymes, what is the difference between a cosubstrate and a prosthetic group? Give one example of each.
Lysine and tryptophan are two amino acids that contain an additional N atom in the R group bonded to the α carbon. While lysine is classified as a basic amino acid because it contains an additional basic N atom, tryptophan is classified as a neutral amino acid. Explain why this difference in classification occurs.
4. Proteases are enzymes that catalyze the hydrolysis of peptide bonds in proteins. The enzyme trypsin is a protease that specifically hydrolyzes only those peptide bonds that are formed by the carboxyl group of basic amino acid residues. Trypsin is present in the small intestine where it functions at an optimum pH of 8. Consider the pentapeptide Phe-His-Val-Lys-Glu. Draw the structures of the products formed from trypsin-catalyzed hydrolysis of this peptide.
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
Amino Acids and Proteins 1. What are the structural features of amino acids with an emphasis on essential amino acids? 2. Write the properties of amino acids: zwitterion, pka, pKb, amphoteric character, isoelectric point, and electrophoresis. 3. Write the mechanism of peptide bond formation and what are its structural features. 4. What are the different types of proteins and their function? 5. Explain the meaning and importance of the primary, secondary, tertiary, and quaternary structures of a protein and the factors that cause its denaturation.
Refer to the bar graph below, Explain why the n→π* interactions contributes more to the overall stabilization of the protein than all the other interactions(C-H-O hydrogen bond,π-π interactions, C5 Hydrogen Bonds, Cation-π interactions, Sulfur-arene interactions, Anion-π interactions, Chalcogen bonds, X-H-π interactions) even though n→π* is the weaker interaction. Explain why that's the case for EACH of the bonds. I.e Why n→π* interactions contribute more to the overall stabilization of the protein than C-H-O hydrogen bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than π-π interactions even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than C5 Hydrogen Bonds, even though n→π* is the weaker interaction. Why n→π* interactions contribute more to the overall stabilization of the protein than Cation-π interactions, even though…
Another method to form a peptide bond involves a two-step process:[1] Conversion of a Boc-protected amino acid to a p-nitrophenyl ester.[2] Reaction of the p-nitrophenyl ester with an amino acid ester.a. Why does a p-nitrophenyl ester “activate” the carboxy group of the first amino acid to amide formation? b. Would a p-methoxyphenyl ester perform the same function? Why or why not?