Please solve... Lys and ArgGlu and LysPro and AspAmong these amino acid combinations listed above, only the combination of Glu and Lys have side chains withgroups that have the greatest ability to stabilize the tertiary structure of a protein.Explain in your own words and by drawing why Glu and Lys side chain interaction stabilizes the tertiary structureof a protein, and why the pairs of Lys and Arg & Pro and Asp cannot provide the stability to the protein structure.

Proteins are composed of a linear chain of amino acids attached together via peptide bonds. All…

Answered: Lys and Arg Glu and Lys Pro and Asp…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 4P

See similar textbooks

Similar questions

Understanding the Relevance of Chaperones in Protein Folding Protein molecules, like all molecules, can be characterized in terms of general properties such as size, shape, charge, solubility/hydrophobicity. Consider the influence of each of these general features on the likelihood of whether folding of a particular protein will require chaperone assistance or not. Be specific regarding just Hsp7O chaperones or Hsp7O chaperones and Hsp60 chaperonins.
Amino acids have the generic structure seen below, where R represents different carbon-based side chains. Describe how the structure of amino acids allows them to be linked into long peptide chains to form proteins.
Protein-4YU4 is given, choose a part of it (containing at least 30 amino acid residues), find the amino acid sequence (sequence in it), identify what functional groups the amino acid substitutes contain (carboxyl group and 2-position the Nitro group will form amide bonds, forming the covalent basic structure of the protein). What different interactions can occur between these functional groups? How will it relate to the spatial structure of the protein?
A fragment of a protein commonly found in food was sequenced and found to have the sequence: RDCEHKY Draw the structure, showing the form expected to be dominant at a physiological pH (7.4). Discuss how changing the pH will affect the fragment, and what implications this has on the overall structure of the protein. What is the difference between the sequence above and the sequence YKHECDR?
Predict the secondary and tertiary structure of the following peptide sequence: a.) LKAENDEAARAMSEA b.) CRAGGFPWDQPGTSN 2.) In an experiment, you somehow added cysteine so that it would covalently bond a protein complex composed of two proteins. But, the problem is you can’t detect the bridge, meaning you can’t detect covalent bond formation of cysteine in between two proteins. How do you generate disulfide bond? Give an idea to force disulfide bond formation between two proteins. 3.)Lysozyme consist of 4 disulfide bridges while Bovine Serum Albumin(BSA) is 17. However, lysozyme is more rigid compared to BSA. Why? What are the factors affecting the rigidity of their structures? Does the number of α-helixes and β-sheets matter?
Alanine has a strong tendency to form α-helix. A biochemist synthesized a polypeptide consisting of 300 alanine residues. When this polyAla300 was suspended in buffered water, it dissolved briefly and then formed a clumped insoluble precipitate that looked like cooked egg-white. Draw a cartoon (simple drawing) of the two different peptides, showing the structural organization of the polyAla300 as an insoluble precipitate, and the structural organization of the soluble (Ala30Gly5)10 polypeptide.
A. Write the structure of the following peptide at pH 5.0 and calculate its net charge at this pH. Asp-His-Tyr-Arg-Lys-Leu-Thr-Gln. Based on the pKa value of the ionizable groups. B. A polypeptide consisting only of L-glutamate residues (poly-L-glutamate) may have a random coil or helical structure depending on pH. Explain this behavior by indicating at what pH values the helical structure will be favored.
Draw the structure of the tri-peptide Leu-Asn-Ser at pH 7.4. Use wedges and dashes around the alpha-carbons, and indicate charges where appropriate. Indicate which amino acid(s) has an R group that would avoid water.
Draw the structure of peptide with the following amino acids Gly-Leu-Ala-Gly-Pro-Hyp. The structure formed of the peptide is most likely a? Please explain. Thank you!
Remembering that the amino acid side chains projecting from each polypeptide backbone in a β sheet point alternately above and below the plane of the sheet, consider the following protein sequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg- Leu-Lys-Ile-Arg-Phe-Glu. Do you find anything remarkable about the arrangement of the amino acids in this sequence when incorporated into a β sheet? Can you make any predictions as to how the β sheet might be arranged in a protein?
Ala-Arg-Val-His-Asp-Gln Given the polypeptide chain above Estimate the net charge of the polypeptide chain at physiological pH (7.4) and at pH 5.0 . How many peptide bonds are there? What kind of polypeptide is it?
The major difference between a protein molecule in its native state and inits denatured state lies in the number of conformations available. To a firstapproximation, the native, folded state can be thought to have one conformation. The unfolded state can be estimated to have three possible orientations about each bond between residues.(a) For a protein of 100 residues, estimate the entropy change per moleupon denaturation.(b) What must be the enthalpy change accompanying denaturation to allow the protein to be half-denatured at 50 °C?(c) Will the fraction denatured increase or decrease with increasingtemperature?

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

SEE MORE TEXTBOOKS