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BIOCHEMISTRY-ACHIEVE (1 TERM)
9th Edition
ISBN: 9781319402853
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 2, Problem 37P
Interpretation Introduction
Interpretation:
The meaning of the statement referring post translational modifications as “Nature’s escape from genetic imprisonment” should be explained.
Concept introduction:
Post-translational modifications are mechanisms which amino acid residues in a protein are covalently modified after protein biosynthesis. For example, phosphorylation is most common post translational modification. Glycosylation and lipidation are also post translational modifications. Proteins are modified by modifying existing
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Students have asked these similar questions
A- what are the Genetic Pathways of organisms? Draw a general of it.
B- define the term posttranslational modification. Why they are important?
Which of the following amino acid types is mostly likely to be hydroxylated in a posttranslation modification on a protein (example: collagen)?
a.) glycine
b.) serine
c.) glutamate
d.) tyrosine
e.) proline
One single polypeptide chain (120 amino acid residues) is produced for protein A in prokaryotic cell. N-terminal amino acid is alanine in the chain of this protein. How many moles of ATP and GTP will be in use for this polypeptide chain synthesis? What post-translational modifications may be for this protein?
Chapter 2 Solutions
BIOCHEMISTRY-ACHIEVE (1 TERM)
Ch. 2 - Prob. 1PCh. 2 - Prob. 2PCh. 2 - Prob. 3PCh. 2 - Prob. 4PCh. 2 - Prob. 5PCh. 2 - Prob. 6PCh. 2 - Prob. 7PCh. 2 - Prob. 8PCh. 2 - Prob. 9PCh. 2 - Prob. 10P
Ch. 2 - Prob. 11PCh. 2 - Prob. 12PCh. 2 - Prob. 13PCh. 2 - Prob. 14PCh. 2 - Prob. 15PCh. 2 - Prob. 16PCh. 2 - Prob. 17PCh. 2 - Prob. 18PCh. 2 - Prob. 19PCh. 2 - Prob. 20PCh. 2 - Prob. 21PCh. 2 - Prob. 22PCh. 2 - Prob. 23PCh. 2 - Prob. 24PCh. 2 - Prob. 25PCh. 2 - Prob. 26PCh. 2 - Prob. 27PCh. 2 - Prob. 28PCh. 2 - Prob. 29PCh. 2 - Prob. 30PCh. 2 - Prob. 31PCh. 2 - Prob. 32PCh. 2 - Prob. 33PCh. 2 - Prob. 34PCh. 2 - Prob. 35PCh. 2 - Prob. 36PCh. 2 - Prob. 37P
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Explain Posttranslational modification of proteins?arrow_forwardMany 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)?arrow_forwardExplain how a peptide bond is formed in translation elongation in terms of: a) Which enzyme catalyzes it b) Where is occurs at the ribosome (EPA sites?) c) What kind of a chemical reaction it is.arrow_forward
- What enzyme catalyzes protein synthesis in bacteria? You discover a new broad-spectrum antibiotic that inhibits protein synthesis and named it Compound J. You want to determine the mechanism of action of Compound J. After treating bacteria cells with Compound J, you observe many ribosomes with long polypeptide chains bound to them. Based on this observation, make a hypothesis about which part of the ribosome Compound J is binding and how this specifically affects translation. What evidence supports that proper protein folding is essential to all domains of life? Name and describe the function/s of two specific molecules that help proteins fold in bacteria.arrow_forwardPost-translational modification of proteins refers to the covalent and enzymatic modification of proteins following protein biosynthesis. Give three (3) examples and briefly describe why the modification is important.arrow_forward4- a) b) data How can bioinformatics tools be used to study posttranslational modifications? By analyzing protein-protein interaction networks By identifying modified peptides in mass spectrometry c) By studying mRNA expression levels d) By investigating posttranslational modification enzyme kinetics e) None of themarrow_forward
- Posttranslational modifications serve several purposes. Discuss and give examplesarrow_forwardIn posttranslational modification, phosphates are attached to which 3 amino acids? - tyrosine - serine - proline - lysine - threoninearrow_forwardOne remarkable feature of the genetic code is that amino acids with similar chemical properties often have similar codons. thus codons with U or C as the second nucleotide tend to specify hydrophobic amino acids. Can you suggest a possible explanation for this phenomenon in terms of the early evolution of the protein-synthesis machinery?arrow_forward
- . The genetic code is thought to have evolved to maximize genetic stability by minimizing the effect on protein function of most substitution muta- tions (single-base changes). We will use the six arginine codons to test this idea. Consider all of the substitutions that could affect all of the six arginine codons. (a) How many total mutations are possible? (b) How many of these mutations are "silent," in the sense that the mutant codon is changed to another Arg codon? (c) How many of these mutations are conservative, in the sense that an Arg codon is changed to a functionally similar Lys codon?arrow_forwardExplain (in one or two lines) the function of the followings:(a) Promoter(b) tRNA(c) Exonsarrow_forwardHow Posttranslational Modifications Regulate Protein Activity ?arrow_forward
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