1. A recent preprint article e reported pre-clinical evaluations of an inactivated Newcastle disease virus (NDV) chimera stably expressing themembrane-anchored form of the SARS-CoV-2 spike region (NDV-S) as a potent COVID-19 vaccine in mice and hamsters. To design the SFChimera, researchers combined the transmembrane domain and cytoplasmic tail of NDV F protein with the ectodomain of the SARS-CoV-2 Sregion, whose sequence is as follows:MGILPSPGMPALLSLVSLLSVLLMGCVAETGTQCVNLTTRTQLPPAYTNSFTRGVYYPDKVFRSSVLHSTQDLFLPFFSNVTWFHAIHVSGTNGTKRFDNPVLPFNDGVYFASTEKSNIIRGWIFGTTLDSKTQSLLIVNNATNVVIKVCEFQFCNDPFLGVYYHKNNKSWMESEFRVYSSANNCTFEYVSQPFLMDLEGKQGNFKNLREFVFKNIDGYFKIYSKHTPINLVRDLPQGFSALEPLVDLPIGINITRFQTLLALHRSYLTPGDSSSGWTAGAAAYYVGYLQPRTFLLKYNENGTITDAVDCALDPLSETKCTLKSFTVEKGIYQTSNFRVQPTESIVRFPNITNLCPFGEVFNATRFASVYAWNRKRISNCVADYSVLYNSASFSTFKCYGVSPTKLNDLCFTNVYADSFVIRGDEVRQIAPGQTGKIADYNYKLPDDFTGCVIAWNSNNLDSKVGGNYNYLYRLFRKSNLKPFERDISTEIYQAGSTPCNGVEGFNCYFPLQSYGFQPTNGVGYQPYRVVVLSFELLHAPATVCGPKKSTNLVKNKCVNFNFNGLTGTGVLTESNKKFLPFQQFGRDIADTTDAVRDPQTLEILDITPCSFGGVSVITPGTNTSNEVAVLYQDVNCTEVPVAIHADQLTPTWRVYSTGSNVFQTRAGCLIGAEHVNNSYECDIPIGAGICASYQTQTNSPSGAGSVASQSIIAYTMSLGAENSVAYSNNSIAIPTNFTISVTTEILPVSMTKTSVDCTMYICGDSTECSNLLLQYGSFCTQLNRALTGIAVEQDKNTQEVFAQVKQIYKTPPIKDFGGFNFSQILPDPSKPSKRSFIEDLLFNKVTLADAGFIKQYGDCLGDIAARDLICAQKFNGLTVLPPLLTDEMIAQYTSALLAGTITSGWTFGAGAALQIPFAMQMAYRFNGIGVTQNVLYENQKLIANQFNSAIGKIQDSLSSTASALGKLQDVVNQNAQALNTLVKQLSSNFGAISSVLNDILSRLDPPEAEVQIDRLITGRLQSLQTYVTQQLIRAAEIRASANLAATKMSECVLGQSKRVDFCGKGYHLMSFPQSAPHGVVFLHVTYVPAQEKNFTTAPAICHDGKAHFPREGVFVSNGTHWFVTQRNFYEPQIITTDNTFVSSGNCDVVIGIVNNTVYDPLOPELDSFKEELDKYFKNHTSPDVDLGDISGINASVVNIQKEIDRLNEVAKNLNESLIDLQELGKYEQYIKGSGRENLYFQGGGGSGYIPEAPRDGQAYVRKDGEWVLLSTFLGHHHHHHHHA. Using the equation on Slide 5.3 of Module 1, Lesson 2, calculate the extinction coefficient (without disulfıdes, in Mcm 1) at 280 nmfor this protein. Show all of your work.B. For each of the following amino acid sequences in the protein, predict the most likely secondary structure. (Is it more likely to be partof an a- helix, ß sheet, a reverse turn, etc.?) Explain why."Note: Although you may use the DSSP algorithm (among others) to provide the prediction, you should still explain what features of the aminoacid sequence make it more likely to be part of a type of secondary structure to receive full credit.1: TNVVIKVC2: SAIGKIQD3: SETKCTLK4: INLVRDLP5: VLHSTQDL6: KIADYNYKC. If you wanted to covalently attach a single fluorescent label to this protein, what are two types of reagents would you use? Be sure togive specific examples, provide details about the chemical mechanism, and explain your choice. EquationsSide S.3.Ea80 (M-' cm-1) == (5500 x nerp) + 1470 x nar) t (125 + nos)Şide li10R- COOH = RC00 + HtK = [RCO0] + [H*][RCOO H]KX acidic[H*]%3D[H*][H*]Slide 1.8pI = ţ Cpk; + pK;)pl(pkit pka)I (pke+ pKz)

"Since you have asked multiple subpart questions, we will solve the first (A) question for you. If…

Answered: A. Using the equation on Slide 5.3 of…

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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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?
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
A. One example of conjugated protein that contains the following Prosthetic groups: a. Iron Protein class, Example, b. Lipids Protein class, Example, c. Phosphate group Protein class, Example, d. Carbohydrate Protein class, Example, е. Heme Protein class, Example,
A. What change should disrupt the interaction between proteins 1 and 2 the most? Why? B. What change would disrupt the interaction between proteins 1 and 2 the least? Why?
Image
Theoretical and experimental data show that in many cases the ionic and hydrogen-bonding interactions to ΔH for protein folding are close to zero. Provide an explanation for this result.
How can I calculate the unknown protein please
if comparing proteins with a Tm=54 degrees C and one with a Tm =78 degrees c, which is more stable
a. Suppose that you have the peptide Ala-Gly-Tyr-His-Leu and you treat it with FDNB and then 6M HCl. Draw the structures of all the products that you will have in solution (assume all reactions to go to completion).
A protein has a dissociation equilibrium constant equal to 4.0um. What is the concentration of free ligand when the fraction of bound sites is 0.7
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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A. Using the equation on Slide 5.3 of Module 1, Lesson 2, calculate the extinction coefficient (without disulfides, in M-1cm 1) at 280 nm for this protein. Show all of your work.