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,...

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Similar questions

Can you please explain how to solve this problem?
A22. Which ONE of the following statements regarding biological molecules is CORRECT? (A) The monosaccharide glucose is predominately in the linear form in aqueous solution. (B) (C) (D) (E) Disaccharides consist of two monosaccharide units linked by an ester bond. Starch is a polymer of glucose units held together by the formation of acetal bonds. Peptides are formed from a number of amino acids bound together through their side chain groups. Peptides and proteins are held together by imine bonds.
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.
Select the correct match : 1.Reducing sugar — Sucrose 2.Phosphodiester bond — Between nucleotides on antiparallel strands of DNA 3.Glycosidic bond — Between repeating units of starch and in glycogen 4.Peptide bond — Formed by elimination of H2 between amino acids
The protein illustrated in the attached picture was isolated from a superhuman being. Scientists theorized that it was the source of power of its power. 1.Give the name of the protein using the one letter symbol.
Your friend has discovered a protein that they suspect is glycosylated. They decide to perform a series of tests to determine the nature of the oligosaccharide. Assuming/Knowing the following: Fucose molecular weight is approximately 164 Galactose molecular weight is approximately 180 GalNAc molecular weight is approximately 221 Mannose molecular weight is approximately 180 Sialic Acid molecular weight is approximately 309 Neuraminidase cleaves before a Sialic Acid (Sialic Acid and anything after leaves the protein) Beta-galactosidase cleaves after a Galactose (Galactose and anything before remains on the protein) Peanut Agglutinin binds to GalNAc Concanavalin A binds to Mannose Hemagglutinin binds to Sialic Acid Based on preliminary results, they suspect that the oligosaccharide is 7 glycosides long and weighs a total of 1414 g/mol They carried out the following experiments: they treated the protein with either a glycosidase or a lectin, and then pelleted the protein using…
9.2
Which of the following statements is incorrect? A.- the structure and charge of the proteins have direct effects on the rate of its migration through the gel matrix include b.- SDS is a type of a buffer with strong protein-denaturing effect and binds to the protein backbone at a constant molar ratio c.- SDS and polyacrylamide gel largely eliminates the influence of the structure and charge, and proteins are separated solely based on polypeptide chain length. d.When proteins are separated by electrophoresis through a gel matrix, smaller proteins appears at the lower portion of the gel
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?
4 This is a three-part question about a tripeptide. Answer all three sub-questions. The pKR of side chains of Tyr, and Lys is 10.46 and 10.54 respectively. The molecular weight of amino acids Ala, Lys, and Tyr in neutral form is 89.1, 146.2, and 181.2 Da, respectively. 1) Draw the chemical structure of the dominant form of tripeptide AKY at pH = 11.5, ensure you have the correct stereochemistry and ionization state of each functional group (Hint, lysine has a C-epsilon as the furthest carbon from C-alpha). 2) Calculate the pI of tripeptide AKY, assuming the terminal amino group has a pKa of 8.0, and the terminal carboxyl group has a pKa of 3.5 3) Calculate the molecular weight of AKY at pI
7. You want to separate these four proteins in a mixture: Isoelectric point Mol. Weight (kDa) Protein A 4.1 80 Protein B 9.0 81 Protein C 8.8 37 Protein D 3.9 172 Which of the following would be the best order in which to run chromatography columns? A) Anion-exchange at pH 3, then size exclusion B) Cation-exchange at pH 3, then size exclusion C) Cation-exchange at pH 3, then anion-exchange at pH 3 D) Anion-exchange at pH 3, then cation-exchange at pH 3 E) Size exclusion, then cation-exchange at pH 3 F) Size exclusion, then anion-exchange at pH 3
1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric 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.

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