1. The use of natural proteins as drugs requires compliance with certain storageand use conditions, which are clearly prescribed in the instructions. So, mostprotein preparations must be stored in a refrigerator at a temperature not excce-ding 10 °C, and dry preparations should be dissolved in boiled water cooled toroom temperature. Some protein preparations are stored in hermetically scaledampoules, from which air is removed. Why do protein drugs require strictadherence to all the conditions prescribed in the instructions, and what canhappen if these conditions are violated?

Protein: Polymer of amino acid joined together through peptide bond removing water in a process…

Answered: 1. The use of natural proteins as drugs…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Bb.45.
The vast majority of structures deposited in the Protein Databank (>95%) have been determined using NMR Hard keratins (such as in the skin) are less resistant to stretch because the larger number of disulfide bonds resist deformative forces. Structures produced by X-ray diffraction are as good as the solutions from which they are derived they are false and I know that but explain why they are false
VII. Analysis of a peptide antibiotic purified from a strain of Bacillus brevii resulted in the following significant information: Complete hydrolysis of the peptide yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val Molecular weight of the peptide was estimated to be aroung 1,200 Da The peptide failed to undergo hydrolysis when treated with carboxypeptidase Partial hydrolysis and then chromatographic separation of products yielded the following di- and tripeptides: Leu-Phe, Phe-Pro, Orn-Leu, Val-Orn, Val-Orn-Leu, Phe-Pro-Val, Pro-Val-Orn Treament with dinitrofluorobenzene (DNFB) followed by complete hydrolysis yielded only free amino acids and the DNFB-derivatized ornithine at its side chain Using this set of information available to you, deduce the amino acid sequence of this peptide antibiotic. Write your final peptide sequence only using 3-letter abbreviations.
1. Complete the table below with information about the amino acids utilized in this pro- cedure. Remember that smaller amino acids will travel further and so will amino acids that are soluble in the solvent. Table 9-1. Amino Acids Procedure AMINO ACIDS Phenylalanine Aspartic Acid Leucine Proline matemps DRAW THE MOLECULAR STRUCTURE in POLARITY (IS IT POLAR OR NONPOLAR?) odme her basalu la MOLECULAR WEIGHT SIZE (RANK LARGEST = 4 AND SMALLEST = 1) SHOULD IT REACT WITH NINHYDRIN?
12 A Aa v AaBbCcDc AaBbCcDdEe AaBbCcDdE AaBbCcDdE Uv ab x, x A A v 三三三=|這、| 4、 Caption Emphasis Heading 1 Heading 3 Q2. Complete the table below with a tick to show which of the following statements describe the molecules. Statement Alpha glucose Fatty acid Amino Nucleotide acid A hexose sugar Insoluble in water Formed by condensation reactions Contain the elements, C, H and Contains the element, N Has a carboxyl group, -COOH Forms polypeptides >
1. The amino acid sequence for the protein lysozyme is given below. Estimate the isoelectric point for lysozyme protein. The pK, values are provided in Table 3.1. KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNT DGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKK IVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL Here's the sequence in this form: LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS ARG HIS GLY Table 3.1 Typical pk, values of ionizable groups in proteins Group Acid Typical pK, Base Terminal a-carboxyl 3.1 group Aspartic acid Glutamic acid 4.1 N. Histidine 6.0 -N + H Terminal a-amino group 8.0 Cysteine 8.3 Тутosine 10.9 + H Lysine 10.8 H H. + N-H Arginine 12.5 N-H N-H Note: Values of pk, depend on temperature, ionic strength, and the microenvironment of the ionizable group. in
Discuss the mechanism that leads to aggregation of a protein therapeutic via a conformationally-altered monomer. Suggest one method of minimising aggregation via the mechanism above. please only answer if you are goin to explain well
1. You need 0.5 liter of a 0.1 M buffer for a biochemical reaction that you plan to perform at pH 2.0. On the shelf in your laboratory you have available phosphoric acid, and the amino acids aspartate, glycine, glutamate, tyrosine, and histidine (all you have available are the fully deprotonated forms of the molecules); these are the only buffer materials you have available. (The pKa values for these compounds are given below.) For phosphoric acid, pKal1 = 2.12, pKa2 = 7.21, and pKa3 = 12.32 For aspartate, pKaCOOH = 1.88, pKaNH3+ = 9.60, pKa sidechain = 3.65 For glycine, pKaCOOH = 2.34, pKaNH3+ = 9.60 For glutamate, pKaCOOH = 2.19, pKaNH3+ = 9.67, pKa sidechain = 4.25 For histidine, pKɑCOOH = 1.82, pKɑNH3+ = 9.17, pKa sidechain = 6.00 For tyrosine, pKaCOOH = 2.20, pKaNH3+ = 9.11, pKa sidechain = 10.07 a. Of these possible buffers, which is likely to yield the greatest resistance to pH change from the starting pH of 2.0, assuming that you were going to run a biochemical reaction that…
1. Sickle cell anemia results from a substitution of a valine for a glutamic acid. What do you expect the effect might be if the mutation were to have placed a leucine at that site? An aspartic acid? 2. Of the following amino acids, glycine, isoleucine, and lysine, which would you expect to be the most soluble in an acidic aqueous solution? Which the least? 3. How many structural isomers could be formed from a molecule with the formula C5H12? C4H8?
Protein a will fold into its native state only when protein b is also present in the solution however protein b can fold itself into native confirmation without the presence of protein a which of the following is true
4. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. (8) mg V₂ μmol s1 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00 0 100 200 300 [s], mM 400 500 WT (a) Estimate the KM and Vmax for the wild-type and mutant enzyme from the graph. V105A (b) Calculate the keat and keat/KM for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
20. The dissociation constant of protein Z for ligand Y is: 10 micromolar. What fraction of the ligand is bound at ligand concentration = 5 micromolar?

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