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)

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Answered: 3. Given the partial sequence of a…

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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i. ii. i.v. 22. Using the figure below, answer the following questions. Identify 2 independent helices domains Identify a disordered region In the structure, box the cofactor and name it (abbreviation accepted) Using the figure, draw the structure of the cofactor bound to this protein
5. Indicate whether the following amino acid residues would be more likely to be found on the surface or in the interior of a folded protein: Leu, Arg, Phe, Asn, and Glu. Give your reasoning for each case (diagrams not required).
Mass spectrometry and X‑ray diffraction are common biochemical techniques for characterizing proteins. Classify each statement based on whether it applies to mass spectrometry, X‑ray diffraction, or both techniques.
Predict the protein 3° structure of the following protein sequence. Provide detail from 2° structure principles Nterm – SLDVTFSPGAEITFKWNPGSFNSLKDTIRQVTDK – Cterm
Page 1 > of 3 ZOOM B. Propose une Toie onsuinin Teguiaung Dioou giucose concentrauon. Question 2: Label the protein structure level on lines 1,2,3, and 4 and label/describe the structure to which each box corresponds. Describe the characteristics of each structural level in the boxes below. MacBook Air DII 80 888 F10 F7 FB F5 F4 F3 * & # $ 7 8 3 4 E R T Y K F M C V .. .. この * 00 B
6. Consider the following proteins to answer the questions below: Protein Size (kDa) pl ε at 280 nm 10 4 7000 50 4 14000 10 8 3000 50 8 50000 A B C C Red Colored? Yes No No No b. Describe a two-step purification procedure that could be used to purify/isolate protein A from the other proteins. In your response, describe the type of chromatography used, the pH of buffer needed, and a labeled chromatogram (include absorbances at both 280 and 400 nm). Make sure you note which "fraction/sample" is needed from the first step to proceed/use for the second step. Use another page if necessary.
#16 please.
2. Would you expect an instrinsically disordered protein to contain a higher proportion of hydrophilic or hydrophobic residues? Explain your reasoning.
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
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?
What would be shortest time a 250 amino acid protein would be able completely fold to the native conformation? [x] micro seconds
5. Refer to Model 2 for information relevant to this question. A sample of the peptide Lys-Glu-Ser has a net charge of zero between what two pH values? What is the pl of Lys-Glu-Ser? Model 2: The pl of a peptide is determined by examining the ionizable groups. The protonated and unprotonated forms of each ionizable group are in equilibrium. Consider the peptide Lys-Glu-Ser shown below at pH 7.2. The complete structure is on on the left and a stylized structure with just the ionizable groups is on the right. While the N-terminal is depicted as protonated, a sample of Lys-Glu-Ser is composed of a population of molecules and within that population some molecules contain a non-protonated N-terminal group at pH 7.2. may H3N* COO- H3N-CH-CIN-CH C N-CH C- H. pK 3.5 OH H. pK= 8.5 COO- CH2 CH2 CH2 NH, pK 10.0 pK 4.2 CH2 CH2 OH CH2 c=0

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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.