Posttranslational modifications of proteins do not include:peptide bond formationglycosylationacetylation of N-terminalpeptide bond cleavagedisulfide bond formationQUESTION 1614 15 16streptomycinpuromycin17 18 19 20Which one of the following antibiotics does NOT function by interfering with the translational/post-translation processtunicamycinpenicillinO tetracyclinOO

Proteins are one of the essential biomolecules for life. These are formed by translation from the…

Answered: Posttranslational modifications 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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Match the antibiotic to its target with bacteria. erythromycin [ Choose ] [Choose ] streptomycin, an aminoglycoside bacterial enzymes involved in folic acid synthesis Bacterial gyrase tetracycline bacterial transpeptidase 70S ribosomes Bacterial RNA polymerase ampicillin Bactrim= trimethoprim + sulfa drug [ Choose ] rifampin [Choose ] ciprofloxacin, a fluoroquinolone [ Choose ] >
Human ribonucleotide reductase has two allosteric sites, the S site and the A site. What is the function of each? How does this compare with the E. Coli enzyme discussed in the text?
What is the difference between eukaryotes and prokaryotes in terms of ribosomal subunit binding?
A sample of an unknown peptide was divided into two aliquots. One aliquot was treated with trypsin and the other was treated with cyanogen bromide. Given the following sequences (N-terminal to C-terminal) of the resulting fragments, deduce the sequence of the original peptide. Trypsin treatment Asn—Tyr—Asp—Met—Phe—Ala—Arg Asp—Trp—Asn—Arg Gln—Met—Tyr—Cys—Pro—Ile—Arg Gln—Cys Cyanogen bromide treatment Tyr—Cys—Pro—Ile—Arg—Asn—Tyr—Asp—Met Asp—Trp—Asn—Arg—Gln—Met Phe—Ala—Arg—Gln—Cys
Why are structural analogs of sugar molecules (such as Oseltamivir and zanamivir) effective in treatment of influenza-virus infection?
match pictures and labels to the correct order in chart
Under what conditions will the following partial diploid strain of E. coli convert chorismate to tryptophan (assume trp mutants function similarly to lac mutants)? trpR* trpP trpO* trpE* trpD* trpC* trpB* trpA*/ trpR trpP trpO° trpE trpD trpC trpB trpA ect the one BEST answer (2 oints! O never O only when tryptophan levels are low O constitutively O only when tryptophan is present O only when chorismate levels are low
What general structural feature is shared by proteins that specifically form homodimers (but not homotrimers, homoteramers etc)? Only one answer is correct. the surface consists of hydrophilic alpha-helix. the surface is highly modified by post-translational modification. the surface is permanently bound by chaperones. the surface is unstructured. the surface, or part of it, is self-complementary.
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
All of the following statements about translation are true except: Release factors recognize stop codons and prompt-cleavage of a peptide bond. Initiation factors are involved in ribosome assembly. In prokaryotes, initiator transfer RNA (tRNAf) is attached to formylmethionine. Each messenger RNA contains a start codon and a stop codon.
Order the following choices to indicate the sequence of steps in the process of elongation of a growing peptide chain. Peptidyltransferase reaction catalyzed by large rRNA subunit. Aminoacyl-tRNA binds the ribosomal A site via EF1x-GTP hydrolysis. EF2-GTP hydrolysis promotes translocation of the ribosome. Release of EF1«-GDP. >

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