2. A functional protein that is approximately 110 kDa in sizehas all its cysteine residues joined with disulfide bonds. Ithas one cysteine residue per 100 amino acids. Whenheated at 85°C it lost activity, but when it was allowed tocool, the activity was restored? Please answer thefollowing questions:a) How many disulfide bonds the protein has? Show howyou came up with the answer.b) What is the molecular basis for the protein behavior inrestoring activity?

Answered: Image /qna-images/answer/cac94dc3-dfa8-4208-be35-8ab28b412de1.jpg

Answered: 2. A functional protein that is…

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

See similar textbooks

Similar questions

A sample mixture consists of three proteins with the following properties: Protein A MW (kDa) 200 Amino acid composition 40% nonpolar, 60% polar B 45 20% nonpolar, 80% polar C 98 85% nonpolar, 15% polar IpH 9 3 5 1. If the mixture is subjected to ammonium sulfate precipitation, which protein will precipitate out first? [Select] 2. If the mixture is subjected to isoelectric focusing, which protein will stop moving nearest to the positive electrode? [Select] 3. If the mixture is subjected to cation-exchange chromatography using a buffer at pH 7, which protein will bind to the resin? [Select] 4. If the mixture is subjected to SDS-PAGE, which protein will be at the bottommost portion of the gel? [Select] * Previous Nex
11. Below is a folding energy funnel describing folding energy landscape of a protein. The width of the funnel indicates the entropy of the protein, and the height corresponds to the free energy. A) If A is the native fold structure, which state is a molten globule? How does this state differ from A in term of structures. B) Does this protein have multiple folding pathways or just one? C) which state has the lowest free energy? D) According to the width of the funnel, the native state B of the protein has the lowest entropy. If the protein fold A spontaneously to this state, does it violate the 2nd law of thermodynamics? Why or why not? (Hint: in the folding funnel, only the entropy of the protein alone is considered). E) Does the native state also have the lowest enthalpy. What makes the enthalpy decrease as the protein folds? 12. List four methods by which a protein can be denatured and briefly describe how these methods act to disrupt protein structure.
Which of the following (could be more than one) would not be a rational explanation for why the three-dimensional structure of a protein is driven and stabilized largely by noncovalent rather than covalent bonds?a) Proteins may be degraded for energy, and if their three-dimensional structures were heldtogether by mostly covalent bonding, this might be too difficult to accomplishb) Proteins will need to be unfolded to cross biological membrane, and if their three-dimensionalstructures were held together by mostly covalent bonding, this might be too difficult toaccomplish.c) Protein function (transport, enzyme catalysis, etc...) may require flexibility in the three-dimensional structure to allow for conformational change, and if protein three-dimensionalstructure were held together by mostly covalent bonding, this might be too difficult toaccomplish.d) All of the answer choices are rational explanations for why the three-dimensional structure of protein is driven and stabilized largely…
a) Draw a non-covalent interaction between a water molecule and the charge on a phosphorylated serine residue(not including backbone atoms). What type of interactuon is this, how strong is it, and what holds the interaction together? b)Draw a non-covalent interaction between an alanine residue and a valine residue(not including backbone atoms). What type of interaction is this, how strong is it, and what holds the interaction together?
It is observed that as temperature is increased, most protein molecules gofrom their defined, folded state into a random-coil, denatured state thatexposes more hydrophobic surface area than is exposed in the folded state.(a) Given what you have learned so far about ΔH and ΔS, explain why thisis reasonable. (b) Sometimes, however, proteins denature as temperature is decreased.How might this be explained?
2) What is glycoside ? In neutral and basic solutions, glycosides do not show mutarotation. However, if the solutions are made acidic, glycosides show mutarotation. Explain why? And write a mutarotation mechanism.
Describe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.
Proteins treated with proteolytic enzymes hydrolyzed peptide bonds to yield a mixture of amino acids only. Is the statement TRUE OR FALSE?
9. At pH ___, the pentapeptide Ala-Glu-His-Val-Cys would contain two positively charged groups and one negatively charged group. a) 9 b) 3 c) 7 d) 1 e) 5
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…
2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu–His–Phe–Arg–Trp-Gly-Lys-Pro–Val-Gly-Lys-Lys-Arg-Arg-Pro–Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu--Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- | Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala 11. - - I C'IL- - 1! (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three peptides would migrate the slowest on SDS-PAGE (g) Which of the three…
13. What value do N-linked saccharides serve for membrane surface proteins? Which amino acid residue(s) do we find involved in N-linked bonds?

SEE MORE QUESTIONS

Recommended textbooks for you

Human Anatomy & Physiology (11th Edition)

Biology

ISBN:

9780134580999

Author:

Elaine N. Marieb, Katja N. Hoehn

Publisher:

PEARSON

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Anatomy & Physiology

Biology

ISBN:

9781259398629

Author:

McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter

Publisher:

Mcgraw Hill Education,

Human Anatomy & Physiology (11th Edition)

Biology

ISBN:

9780134580999

Author:

Elaine N. Marieb, Katja N. Hoehn

Publisher:

PEARSON

Biology 2e

Biology

ISBN:

9781947172517

Author:

Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:

OpenStax

Anatomy & Physiology

Biology

ISBN:

9781259398629

Author:

McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter

Publisher:

Mcgraw Hill Education,

Molecular Biology of the Cell (Sixth Edition)

Biology

ISBN:

9780815344322

Author:

Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter

Publisher:

W. W. Norton & Company

Laboratory Manual For Human Anatomy & Physiology

Biology

ISBN:

9781260159363

Author:

Martin, Terry R., Prentice-craver, Cynthia

Publisher:

McGraw-Hill Publishing Co.

Inquiry Into Life (16th Edition)

Biology

ISBN:

9781260231700

Author:

Sylvia S. Mader, Michael Windelspecht

Publisher:

McGraw Hill Education

SEE MORE TEXTBOOKS