3. Given the partial sequence of a peptide:ILWANRMSHVLFAVE AWhich amino acid residues would you expect to be on the solvent-exposed surface once it foldinto its native conformation (in vivo)? State your reasoning in full sentence. The following data is protein melting point (Tm) characterization data obtained by the ZetasizerNano System (Dynamic Light Scattering method, DLS)². The melting point for the series of proteinsare measured in PBS (phosphate buffered saline). Which protein is structurally the most stableform in PBS? State your reasoning in full sentence.Z average in DLS: The dynamic size of particle.100ProteinBovine HemoglobinBovine Serum AlbuminOvalbuminHuman InsulinHen Egg LysozymeT.(°C)9038657164688070605040302010-3035404550556065707580Temperature (°C)Z Average Diameter (nm)

3. Given the partial sequence of a peptide: ILWANRMSHVLFAVE A Which amino acid residues would you expect to be on the solvent-exposed surface once it fold into its native conformation (in vivo)? State your reasoning in full sentence.

3. Given the partial sequence of a peptide: ILWANRMSHVLFAVE A Which amino acid residues would you expect to be on the solvent-exposed surface once it fold into its native conformation (in vivo)? State your reasoning in full sentence.

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter3: Biological Molecules: The Carbon Compounds Of Life

Section: Chapter Questions

Problem 8TYK: The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices...

See similar textbooks

Related questions

Q: Draw the peptide chain (indicate if it is solid or hatched wedges) for the following and compute for…

A: Polypeptide molecules are composed of a sequence of amino acids where an amino group of each amino…

Q: Why do we need to study the four levels of protein structure? Cite its practical use to our…

A: Protein structure is a complicated structure made of many amino acids linked together by peptide…

Q: 3. Quaternary protein structures are formed by spontaneous assembly of individual polypeptides a.…

A: Disclaimer: Since it is not mentioned which question is to be attempted, only the first question is…

Q: 4. Draw the example of Ramachandran plot for: A) regular secondary structure (4=60-65; y-60-80) B)…

A: Ramachandran plots depict the combination of backbone dihedral angles and statistical distribution.…

Q: 2. Draw the structural formula of the amino acid asparagine that predominates in solution at each of…

A: Asparagine is a polar amino acid. It contains one amide group in its side chain which is not…

Q: 5. The tertiary structure of a protein involves attractions and repulsions between the side chain…

A: The tertiary structure of the protein is stabilized by two types of bonds. 1. Covalent bond: The…

Q: 1. What is Amino Acid and its relation to proteins? 2. What is the importance of using multiple…

A: Since there are two questions asked, we will solve them both.

Q: 2. PICK ONE: Decide whether you will use peptide YAD or peptide SHY а. What are the amino acids (in…

A: Let's choose peptide YAD. pKa of carboxyl group (aspartic acid) = 1.88 pKa of side chain group…

Q: 4. The table below describes a procedure in preparing standard solutions of a protein sample with…

A: Proteins are chain of amino acids linked by the peptide bonds, a covalent bond. Its concentration…

Q: 4. Draw the bond-line structure of the peptide that corresponds with the following sequence of amino…

A: Polypeptides are the long chain of the monomer units of amino acids, which are joined by peptide…

Q: 1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this…

A: Chromatography is a separation technique that is used to separate components of a mixture based on…

Q: 1) What is the charge state of the peptide in pH7 water solution? a GKEAPLCKR

A: Hi, First I would like to thank for submitting a question. As you have multiple question here and we…

Q: Amino acid Ala Asp Arg Cys a-carboxyl group a-amino group pK a pK a 2.35 9.78 1.99 9.90 1.82 8.99…

A: There is a characteristic pH of any amino acid at which their net electric charge becomes zero, it…

Q: 1. Using Hydrophobic interaction chromatography, the protein that will be eluted FIRST is

A: Hydrophobic interactions are one typeof bonding interactions that are present between water and…

Q: 4) Using the pK, data found in the supplied chart, determine the predominant charge of each amino…

A: Amino acid is amphoteric in nature i.e it can act as both acid as well as . This property is due…

Q: A researcher performed an SDS-PAGE experiment (with 2- mercaptoethanol) on a mixture containing 3…

A: G

Q: 9) How many peptide fragments would you expect to generate from reacting the following amino acid…

A: Trypsin cleaves the peptide bond between the carboxyl group of arginine or the carboxyl group of…

Q: Which of the following is incorrect about the beta sheet? Parallel beta sheets are less stable than…

A: In a protein the polypeptide chains have four levels of structural organization and they are…

Q: 1. Please draw the given peptide and calculate the net charge at pH 1, 4, 8 and 12. GRNVGHEWA

A: A peptide can be defined as a short chain of amino acids. They are connected to each other by a…

Q: 3. Three dipeptides were separated by paper electrophoresis at pH 6.4 and the results are shown…

A: Natural proteins or peptides are composed of twenty standard amino acids attached together via…

Q: 2. Calculate the pI of the following primary structure of protein A) Lys- Gly- Ala- Gly B) Lys-…

A: Since you have asked a question with multiple subparts, we will answer first 3 subparts for you. In…

Q: 7. A peptide has the sequence Cys-His-Glu-Met-lle-Ser-Thr a. Write out the single letter sequence of…

A: Note: We are authorized to answer one question at a time since you have not mentioned which question…

Q: 4. A particular amino acld inside or the outside of the folded protein? Briefly explain. on the

A: Amino acid in nature has the same fundamental structure. It consists of a carbon atom, the alpha (α)…

Q: 4. a. Give the full names of the amino acids in this peptide. H3 N -CH-C-N-CH-C-N-CH- C ČH3 н Cнон н…

A: The pKa values of amino acid side chains that constitute a protein play an important role in…

Q: Fill in the blank: Identify the type of non-covalent/covalent interactions present in the following…

A: The Ramachandran plot also termed as Rama plot is the way to visualize the position of backbone…

Q: Look at the schematic illustration of a protein (3D conformation) belpw. If the highlighted SER…

A: Proteins are the biomolecules that are made up of Aminoacids joined by Peptide bond. Proteins exist…

Q: The enzyme thermolysin cleaves peptide bonds on the C-terminal side of the amino acids lle. Tyr,…

A: Amino acids are monomeric units that form a peptide chain. The amino acids are linked together by a…

Q: In relation to the peptide sequence that is presented. -Gly - Ser – Cys – Asp – Glu – Arg – Cys –…

A: The given peptide sequence contains 8 amino acids. In a peptide, individual amino acids are joined…

Q: Having peptides arranged in a beta sheet would be an example of a secondary structure A) True B)…

A: Peptides and polypeptides are linear and unbranched polymers composed of amino acids linked together…

Q: 6. An allosteric enzyme has which of the following properties? 1. It can only operate in an acidic…

A: Allosteric enzymes are the enzymes that changes their conformation according to the binding of…

Q: Describe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note…

A: Biomolecules are organic molecules made up of mainly carbon and hydrogen, but other elements are…

Q: 3. Which of the following processes involves the loss of a protein’s native structure?…

A: Proteins are polypeptides made up of amino acids. The biochemically and structurally stable form of…

Q: 6. How are amino acids linked together in a protein molecule? Write the general structure of the…

A: Amino acids are the molecules that join to form a protein structure. The bond formed between two…

Q: 2. Fill in the blank: Identify the type of non-covalent/covalent interactions present in the…

A: The Ramachandran plot is a graph plot between phi (φ) and psi (ψ) the torsional angles of the…

Q: 2. Why would a protein have an apparent size of 40 kDa (kiloDaltons) at pH 6.5 but when the protein…

A: Proteins are the linear polymers of amino acids attached together via peptide bonds. There are…

Q: The three-dimensional conformation of a protein may be strongly influenced by amino acid residues…

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

Q: 4. Show exactly which peptide bonds you would expect trypsin to cleave if you set a digest with the…

A: Enzymes are protein molecules that increase the rate of biochemical reactions. Trypsin is an enzyme…

Q: Discuss the mechanism that leads to aggregation of a protein therapeutic via a…

A: Misfolded proteins acquire a shape that causes polymerization into aggregates and structured…

Q: e configuration of a protein molecule? Provide an exam

A: Protein characteristics are determined not only by the sequence of amino acid residues in…

Q: betaME on protein structure. The proteins don't contain any cysteine residues in its primary…

A: We are answering first question. For other question pls repost.

Q: e subsequent residue e peptide bond is freely rotatable along its bond axis e peptide bond contains…

A: In a protein various amino acids are linked together by a peptide Bond formation. This bond…

Q: Suppose you are working with a protein who's native structure contains an highly conserved valine…

A: A protein molecule is made up of a specific sequence of amino acids. The sequence of amino acids…

Q: Describe in detail how to detect the primary structure of protein.

A: Hello! Since you have posted multiple questions, we are answering only first question. If you need…

Q: Currently working on protein structures and am having difficulty understanding the principles behind…

A: Polypeptide chain folds due to interactions between the functional groups present in the amino acids…

Q: What is the key driving force for forming stable 3D structures of proteins (e.g., the coronavirus…

A: 3-D structures of proteins are the tertiary and quaternary protein structures that are the final…

Q: Which best describes the contribution of quaternary (4’) structure of polypeptides to the native…

A: Option B The quaternary structure of Proteins is formed by noncovalent forces binding the subunits…

Q: 7. Give the 2 examples of each of the followings:- (a) hydrophilic amino acid, (b) Charged AA, and…

A: Amino acids can be classified depending on the side chain/group it possess. hydrophilic/polar amino…

Q: ii Between structures (a) and (c), which one would have the following amino acid (pictured below)…

A: Proteins are molecules composed of amino acids joined together by peptide linkages. There are three…

Q: Given the partial sequence of a peptide: ILWANRM SHVLFAVE A Which amino acid residues would you…

A: The process when a polypeptide chain folds into three-dimensional configuration, where it is stable…

Question

3. Given the partial sequence of a peptide:
ILWANRMSHVLFAVE A
Which amino acid residues would you expect to be on the solvent-exposed surface once it fold
into its native conformation (in vivo)? State your reasoning in full sentence.

The following data is protein melting point (Tm) characterization data obtained by the Zetasizer
Nano System (Dynamic Light Scattering method, DLS)². The melting point for the series of proteins
are measured in PBS (phosphate buffered saline). Which protein is structurally the most stable
form in PBS? State your reasoning in full sentence.
Z average in DLS: The dynamic size of particle.
100
Protein
Bovine Hemoglobin
Bovine Serum Albumin
Ovalbumin
Human Insulin
Hen Egg Lysozyme
T.(°C)
90
38
65
71
64
68
80
70
60
50
40
30
20
10-
30
35
40
45
50
55
60
65
70
75
80
Temperature (°C)
Z Average Diameter (nm)

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

Step 2

Step 3

Step 4

Trending now

This is a popular solution!

Step by step

Solved in 4 steps

SEE SOLUTION Check out a sample Q&A here

Similar questions

2. Would you expect an instrinsically disordered protein to contain a higher proportion of hydrophilic or hydrophobic residues? Explain your reasoning.
1. Draw the peptide chain (indicate if it is solid or hatched wedges) for the following and compute for the isoelectric point. Show solution. Glycine-(L)-Arginine-(D)-Proline-(L)-Glutamic Acid
The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this information, list all the polar amino acids and arrange them from most polar to least polar.
1. Use the info of this molecule as well as the attached addendum to demonstrate the flow of genetic information to protein sequence as described by the so-called “Central Dogma” . Clearly indicate the direction of your polynucleotide strands and peptide/protein. ATG GCA TGC AAT AGC TCA TGC 2. What would happen to the amino acid sequence if the underlined nucleotide (C) would change to an A?
1. outline the principles and procedures of isoelectric focusing. 2. Explain the four levels of protein structure.
The three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.
4. Amino acids are linked together by peptide bonds to form polypeptides. (a) Draw the structure of a tripeptide (b) draw an asterisks (*) directly beside all alpha carbons and draw a square around all peptide bonds (c) Use arrows to identify and label the N-terminus and C-terminus (d) Draw a circle around the R group of each amino acid residue in the tripeptide and classify each R group as polar, non polar, acidic, or basic (e) Using the abbreviated names of the amino acids, provide the primary structure of the tripeptide you have drawn.
A peptide containing 18 amino acid residues in its sequence was partially hydrolyzed and peptides A–D were detected in the resulting mixture. Draw the sequence of the original peptide.A Phe-Gly-AlaB Ser-Ser-Ser-Trp-Phe-Gly-AlaC Phe-Phe-Met-Ala-Ala-Pro-Trp-CysD Met-Ala-Ala-Pro-Trp-Cys-Leu-Ile-Leu-Ser-Ser
1. Which peptide would be more soluble at pH 7.0, (Val)₂₀ or (Asp)₂₀ ? at pH 3.0, (Gly-Glu-Val)
1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic point of the amino acids are as follows: histidine:7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.
When will scientists be able totake any amino acid sequence andaccurately predict both that protein’sthree-dimensional conformationsand its chemical properties? Whatbreakthroughs will be needed toaccomplish this important goal?