on-fionSubstituting antisense oligonucleotide non-bridging oxygen atoms with a sulpha atom:Select one:O a. Decreases oligonucleotide stability in biological fluidsO b. Increases oligonucleotide hydrophobicity increasing the likelihood of it partitioning aO c.None of theseOd.Increases oligonucleotide stability in biological fluidsOe. Has no effect on oligonucleotide stability in biological fluidsTherapeutic replacement genes need to be delivered to which intracellular compartment?Select one:O a. The chloroplastO b. The lysosomeThe NucleusO c.O d. The ribosomeO e.The GolgiGive both answer only with little bitexplanationAsapThanks

Ans. 1. Option d is correct The antisense nucleotide non bridging oxygen atom replace by the sulphur…

Answered: Substituting antisense oligonucleotide…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 17P

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H8. Protein A interacts with biomolecule B and forms a complex AB, with a dissociation constant KD = 1 µM at 25 °C, (for dissociation, AB ⇋ A + B, KD=[A][B]/[AB]). The interface contains a phenylalanine residue. A biochemist mutated the phenylalanine of protein A to a tyrosine (A’), which introduced a hydrogen bond between the hydroxyl group of the tyrosine with B without affecting any other interactions. The formation of the hydrogen bond releases a heat at 11.4 kJ/mol. What is the KD of the complex of the mutant A’ with B? Hint: Gas constant R = 8.3145 J/K/mol, Euler’s number e = 2.7183, ln(A) - ln(B) = ln(A/B).
In SDS polyacrylamide gel electrophoresis, which of the following polypeptides move slowest?A) The ones with the lowest molecular weightB) The ones with the highest molecular weightC) The most negatively chargedD) The most positively chargedE) The ones with the lowest buoyant density
A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown here. Only one of the Cys has a free —SH group, and the other two are involved in an —S—S— bond. The only methionine and the only aromatic amino acid (Phe) in this protein are in the positions indicated. Cleavage of the intact protein (i.e., withdisulfide bonds intact) by either cyanogen bromide or chymotrypsin does not break the protein into two peptides. Where is the —S—S— bond (i.e., AB, BC, or AC)?
Given a tripeptide Cys-His-Lys, Cys: Pk1 = 1.5; Pk2 = 10.8; PkR = 8.5 His: Pk1 = 1.6; Pk2 = 9.0; PkR = 7.0 Lys: Pk1 = 2.2; Pk2 = 8.5; PkR = 9.8 a.draw the protonic equilibria for the tripeptide. b.what is the IpH? c.What is the dominant structure at pH 3.0? d.What is the first buffering region of the tripeptide?
In the deoxy state of HB, which of the following does not occur? a) An inter-chain salt bridge between Histidine 146 and Lys 40 b) An intra-chain salt bridge between Val 98 and Tyr 145. c) An intra-chain salt bridge between Histidine 146 and Aspartate 94 side chains d) A peptide bond between Tyr 145 and His 146.
a. Why is it important to eat food containing antioxidants? Write at leasttwo reactions to prove the answer. b. Write in four ways the following nucleotide sequence: ATGCA. c. Explain i. Hoogsteen pairing & ii. Hyperchromic effectiii. Epimers Iv. Mutarotaton v. Aldose vi. Anomers vii. Mutarotation
Parallel beta sheets are less stable than antiparallel beta sheets, becasue they have __________ hyrdogen bond. Fill in the blank less or more?
2. It is known hemoglobinopathies, whi ch arise due to mutations in one of histidines a- or B- chains binding with the iron in the heme gro up.These mutations stabilize the iron in Fes form. Some drugs (eg. sulfonamides) or chemicals( eg.anilin) also can cause methemoglobinemia. Suggest, how change the properties of Hb in these cas es. For this:1)Describe the structure and function of Hb A as a transport protein. 2) Explain the role ofiron ions in act ive centers of Hb for the binding of O23) How many molecules of Oz can bind mutant Hb, if mutation occurs in a- subunits? 4) Why can ascorbic acid be used to tr eat of such patients.
Need both answer ASAP. 1.Draw the structure of pppUCGAP ribonucleic acid in the ionic form that would predominate at pH 7.0. 2.Draw the structure of ppTGACpp deoxyribonucleic acid in the ionic form that would predominate at pH 7.0.
Mutations are caused by chemical and physical phenomena. Indicate the type of mutation that each of the following reactions or molecules might cause: a. ROS b. intercalating agents c. a small alkylating agent d. a large alkylating agent e. nitrous acid
In the image attached, there are 4 nitrogenous bases plus ribose used to generate strands of DNA. They are oriented with hydrogen bonding regions aligned. A. Diagram the chemical structure of cytosine hydrogen-bonded to guanine in normal DNA. Please show the H bond interactions clearly with a dotted line. B. In a second diagram, show the enol form of cytosine following a tautomeric shift. Include in the diagram how this change shifts hydrogen bonding characteristics and a new binding partner for this nucleotide.
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Substituting antisense oligonucleotide non-bridging oxygen atoms with a sulpha atom: Select