The alkaline hydrolysis of pAUGCAGC oligonucleotide produces:O A. Uridine 2'-monophosphate, uridine 3'-monophosphate, cytosine 2'-monophosphateO B. Adenosine 2'-monophosphate, adenosine 3'-monophosphate, adenosine 21,5'-bisphosphateOC. Guanosine 2'-monophosphate, guanosine 3'-monophosphate, cytosine 3'-monophosphateO D. Cytidine 3'-monophosphate, guanosine 2'-monophosphate, adenine 2'-monophosphateO E. Adenine 3,5'-bisphosphate, guanine 2,5'-bisphosphate, uridine 2'-monophosphateO F. Uridine 2'-monophosphate, uridine 3'-monophosphate, guanine 3'-monophosphate

Alkaline hydrolysis is a process by which RNA is degraded dur to attack of -OH ions of alkali. The…

Answered: The alkaline hydrolysis of pAUGCAGC…

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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Which of these amino acids is a polar, uncharged amino acid? (Select all that apply, if necessary.) A. B. D. E. CHLO H₂N-CH-C CH₂ CH₂ CH₂ NH C=NH2 NH₂ amino acid A amino acid C amino acid D amino acid B amino acid E H₂N-CH-C CH₂ _i_g C. H₂N-CH-C- CH2₂ I CH₂ =0 NH₂ H₂N-CH- CH₂ CH-CH3 CH3 H₂ND H₂N-CH- | CH₂ Ï OH
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Consider the peptide in the image and answer the following questions.
Name the structure below: A. Adenosine B. Cytidine C. Thymidylate D. Adenylate
1. Label the ALPHA-Carbon, AMINO Group, CARBOXYL Group, and AMINO Side Chain of the following amino acids:- Proline- Glycine- Aspartic acid- Asparagine- Lysine 2. Write the structure of the following polypeptide chainsa.) Asp-Leu-Serb.) Thr-Trpc.) Gln-Ala-Prod.) Ile-Met-Cys-Glu
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17. Melittin is a 26-amino acid polypeptide found in bee venom. In its monomeric form, melittin is thought to insert into lipid-rich membrane structures. Explain how the amino acid sequence of melittin accounts for this property. 1 Gly-le-Gly-Ala-Val-Leu-Lys-Val-Leu-Thr-Thr-Gly-Leu-Pro 25 NH GIn-Gln-Arg-Lys-Arg-Lys-le-Trp-Ser-le-Leu-Ala
You are presented with Cytidine 5' triphosphate and Thymidine 5' triphosphate. Draw and upload to Efundi these phosphorylated structures as they would be connected in a polinucleotide in the order CpT / Show the individual phosphorylated structures first then show how they combine to form the polynuleotide. Show at any one of these structures where the glycosidic bond occurs
Consider the hydrogen bonding pattern of an α-helix with the following sequence: HLRTNAGCSY Asparagine’s amide hydrogen is hydrogen bonded to: a. Serine’s side chain b. Histidine’s backbone carbonyl oxygen c. Cysteine’s backbone carbonyl oxygen d. Serine’s backbone carbonyl oxygen e. Histidine’s side chain
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…
Imagine that a mutation has been discovered in the HBA1 gene, where amino acid residue # 1 in the alpha subunit is changed from valine to lysine. The structure of these two amino acids is shown below. How would this mutation affect the mobility of HbA in the gel?a) HbA with this mutation would have the same mobility as normal HbAb) HbA with this mutation would have the same mobility as HbSc) HbA with this mutation would have a faster mobility than normal HbA O d) HbA with this mutation would have a mobility somewhere in between HbS and normal HbA

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