A random-sequence polyribonudeotide produced by polynudleotidephosphorylase, with CDP and ADP in a 5:1 molar ratio stimulated theincorporation of proline, histidine, threonine, glutamine, asparagine, and ly-sine in a cell-free translation system in the following proportions: 100, 23.4,20, 3.3, 3.3, and 1.0, respectively. What does this experiment reveal about thenucleotide composition of coding triplets for these six amino acids?

Amino acids are coded by a tripeptide sequence called codons. The first two positions of the codon…

Answered: A random-sequence polyribonudeotide…

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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Given the following diagram of how protein AWESOME1 binds to it's target DNA, describe the potential effects of each of the 5 mutations shown below. The wild-type sequence of a helix #1 is also shown in the blue box, and all the mutations are in helix #1 (see numbers for identifying particular residues). a helix #1 R(1)-V-I-L-Y-F-W-I-M-Y-F-S-H-Y-W-R(16) #1 Predict the consequence of the following mutations: 1) Arg(1) to Glu 2) Arg(1) to Ala 3) Phe(6) to lle 4) Trp(7) to Phe 5) Met(9) to Pro in
Many blood clotting proteins undergo a post-translational modification in which specific glutamic acid residues (Glu) in the protein are converted to gamma-carboxyglutamic acid residues (Gla). See reaction scheme below. An example is the blood clotting protein Factor IX, which has 12 Glu in its N-terminus converted to Gla. This modification gives Factor IX the ability to bind calcium and phospholipid membranes. Bacteria do not have the enzyme required to convert Glu to Gla and therefore Factor IX proteins expressed in bacteria would not have the proper modifications. How might you engineer the translational apparatus of a bacterial cell line so that it produces Factor IX with Gla in the appropriate positions. How would you ensure that only the 12 Glu in Factor IX that are normally converted to Gla and not just all Glu (Limit 5-6 senetnces)?
Referring to the genetic code presented in Figure , give the aminoacids specified by the following bacterial mRNA sequences. Q. 5′ –UUUGGAUUGAGUGAAACGAUGGAUGAAAG AUUUCUCGCUUGA–3′
Wild-type E. coli cells can synthesize all 20 common amino acids, but some mutants, called amino acid auxotrophs, are unable to synthesize a specific amino acid and require its addition to the culture medium for optimal growth. Besides their role in protein synthesis, some amino acids are also precursors for other nitrogenous cell products. Consider the three amino acid auxotrophs that are unable to synthesize glycine, glutamine, and aspartate, respectively. Match each nitrogenous product with the mutant or mutants that would fail to synthesize it. Each mutant may fail to synthesize more than one nitrogenous product, and some nitrogenous products may fail to be synthesized by more than one mutant. glycine auxotrophs glutamine auxotrophs aspartate auxotrophs Answer Bank adenine nucleotides cytosine nucleotides guanine nucleotides uridine nucleotides
A mixture of four a-[*p]-labeled ribonucleoside triphosphates was added to permeabilized bacterial cells undergoing DNA replication in the presence of an RNA polymerase inhibitor, and incorporation into high-molecular- weight material was followed over time, as shown in the accompanying graph. After 10 minutes of incubation, a 1000-fold excess of unlabeled ribo- nucleoside triphosphates was added, with the results shown in the graph.
A peptide with the primary structure Lys-Arg-Pro-Leu-Ile-Asp-Gly-Ala must be synthesized by the methods developed by Merrifield. Calculate the percentage of the peptides synthesized that will be full length and have the correct sequence if the addition of each amino acid residue is 96% efficient. Do the calculation a second time but assume a 99% efficiency for each cycle. full-length peptides with the correct sequence if 96% efficient: full-length peptides with the correct sequence if 99% efficient: % %
A double-stranded fragment of viral DNA, one of whose strands is shown below, encodes two peptides, called vir-1 and vir-2. Adding this double-stranded DNA fragment to an in vitro transcription and translation system yields peptides of 10 residues (vir-1) and 5 residues (vir-2). Solve, (b) Determine the amino acid sequence of each peptide.
A mixture of four a-[32P]–labeled ribonucleoside triphosphates was added to permeabilized bacterial cells undergoing DNA replication in the presence of an RNA polymerase inhibitor, and incorporation into high-molecular-weight material was followed over time, as shown in the accompanying graph. After 10 minutes of incubation, a 1000-fold excess of unlabeled ribonucleoside triphosphates was added, with the results shown in the graph. Incorporation of radioactivity, cpm Excess (a) Why was the excess of unlabeled rNTPs added?(b) How could you tell that radioactivity is being incorporated as ribonucleotides rather than as an alternative such as reduction to deoxyribonucleotides, followed by incorporation?(c) What does this experiment tell you about the process of DNA replication?
A mixture of four a-[32P]–labeled ribonucleoside triphosphates was added to permeabilized bacterial cells undergoing DNA replication in the presence of an RNA polymerase inhibitor, and incorporation into high-molecular-weight material was followed over time, as shown in the accompanying graph. After 10 minutes of incubation, a 1000-fold excess of unlabeled ribonucleoside triphosphates was added, with the results shown in the graph. (a) Why was the excess of unlabeled rNTPs added?(b) How could you tell that radioactivity is being incorporated as ribonucleotides rather than as an alternative such as reduction to deoxyribonucleotides, followed by incorporation?(c) What does this experiment tell you about the process of DNA replication?
The genetic code was solved partly by the use of in vitro systems to translate synthetic RNAs into peptides. In these systems, ribosomes, amino acids, and buffers that support translation are added and there is no control of where translation begins. AAA = Lys; AUA = Ile; AAU = Asn; UAA = stop. What peptides would NOT be produced in an in vitro system if the following oligonucleotide were added: AAAAAAAAAUAAAAAAAA Select one: a) Lys-Lys-Lys-Lys-Lys-Lys-Lys-Lys b) Lys-Lys-Ile-Lys-Lys c) Lys-Lys-Asn-Lys-Lys
Using the pKa data in as shown and the Henderson-Hasselbalch equation,calculate the approximate net charge on each of the four common ribonucleoside 5′-monophosphates (rNMPs) at pH 3.8. If a mixture of these rNMPs was placed in an electrophoresis apparatus, as shown, draw four bands to predict the direction and relative migration rate of each.
Second Letter U A G | Phe UCU UUC UUA Tyr UGU UGC Cys /u Stop UGA Stop | A Stop UGG Trp G UUU UAU UAC UCC Ser | UCA UAA Leu UUG UCG UAG CU Leu ccc CAU CAC CAA CUU His CGU CUC CGC | Arg | C Pro CUA CCA Gln CGA A CUG CCG CAG CG AGU Ser U AUU AUC ACU ACC AAU Asn Thr AAC AAA lle AGC AUA АCА AGA | Lys A Arg G AUG Met | ACG AAG AGG GUU GUC GCU GAU GAC Asp GGU GGC GGA U Val |GCC GCA Gly C A Ala GUA GAA Glu GUG GCG GAG GGG G

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