Rank from left to right the compoundwith the most reactive chemicallinkage: peptide bond, ester, ether, acidanhydride, aminoacyl-TRNAHow many bacterial translation factorsare "G" proteins?How many proteins are involved in thenucleotide-dependent steps of proteinsynthesis?

There are different types of biomolecules found in nature. Various forms of biomolecules include…

Answered: Rank from left to right the compound…

Rank from left to right the compound with the most reactive chemical linkage: peptide bond, ester, ether, acid anhydride, aminoacyl-TRNA

Human Heredity: Principles and Issues (MindTap Course List)

11th Edition

ISBN:9781305251052

Author:Michael Cummings

Publisher:Michael Cummings

Chapter9: Gene Expression And Gene Regulation

Section: Chapter Questions

Problem 15QP

See similar textbooks

Related questions

Q: Н H₂N-C-COOH CH2 CH2 CH₂ M OW Oc

A: Amino acids are chemical molecules that combine to produce proteins and are hence known as building…

Q: Provide the correct three-letter abbreviation for the following amino acid: O H₂N-CH-C-OH CH₂ CH₂…

A: Amino acids are the building blocks of proteins. They are organic compounds composed of an amino…

Q: The above glucose monosaccharides are held together in the maltose sugar by: glycosidic bonds ether…

A: An Ether has two carbon atom that are bonded with oxygen with single bond. For example, dimethyl…

Concept explainers

Nucleotides

It is an organic molecule made up of three basic components- a nitrogenous base, phosphate,and pentose sugar. The nucleotides are important for metabolic reactions andthe formation of DNA (deoxyribonucleic acid) and RNA (ribonucleic acid).

Nucleic Acids

Nucleic acids are essential biomolecules present in prokaryotic and eukaryotic cells and viruses. They carry the genetic information for the synthesis of proteins and cellular replication. The nucleic acids are of two types: deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). The structure of all proteins and ultimately every biomolecule and cellular component is a product of information encoded in the sequence of nucleic acids. Parts of a DNA molecule containing the information needed to synthesize a protein or an RNA are genes. Nucleic acids can store and transmit genetic information from one generation to the next, fundamental to any life form.

Question

Rank from left to right the compound
with the most reactive chemical
linkage: peptide bond, ester, ether, acid
anhydride, aminoacyl-TRNA
How many bacterial translation factors
are "G" proteins?
How many proteins are involved in the
nucleotide-dependent steps of protein
synthesis?

Expert Solution

This question has been solved!

Explore an expertly crafted, step-by-step solution for a thorough understanding of key concepts.

This is a popular solution!

SEE SOLUTION Check out a sample Q&A here

Step 1

VIEW

Step 2

VIEW

Step 3

VIEW

Trending now

This is a popular solution!

Step by step

Solved in 3 steps

SEE SOLUTION Check out a sample Q&A here

Knowledge Booster

Learn more about

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

Sketch the following two tripeptide chains: Asp-Gly-Ser and Ile-Asn-Met at physiological pH . Please provide only typed answer solution no handwritten solution needed allowed
Which of the choices are types of posttranslational modifications a newly synthesized protein may undergo? Select all the choices that apply. changes to hydrogen bonding capabilities formation of an amide bond between Cys and an isoprenyl group removal of prosthetic groups removal of the thiol group from a Cys residue modulation of charges on amino acids proteolytic cleavage covalent attachment of oligosaccharides to Asn, Thr, or Ser
Can you please describe the specific components that each of these structures are comprised of ( alpha helices and beta sheets) in more detail? Also, what do the different colors represent? Your reply will be greatly appreciated. The ligand that was assigned to me is tadalafil.
To visualize the spatial arrangement of amino acid residues in an a-helix, it is helpful to imagine you are looking down the long axis of the helix, just as you would look down a soda straw. Viewed in this orientation, the residues form a circle, with each residue offset from its neighbor by 100 degrees. This representation is called a helical wheel. Use the circle below to indicate the position of each residue around the helix of the enzyme lysozyme. NH ...Arg - Cys - Glu- Leu - Ala Ala - Ala Met-Lys COO- The first two amino acids, Arg-1 and Cys-2, are shown as an example. Arg-1 O Glu-3 Which amino acid in the polypeptide is the first to pass the origin (i.e., which amino acid passes Arg- 1 first, completing one full circle)? Select the best answer. O Leu-4 O Ala-5 O Ala-6 O Ala-7 Met-8 O Lys-9 100° O none of the above Cys-2
Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.
Briefly describe each of the following possible posttranslational protein modifications. Give an example of each. Cross-linkage glycosylation and phosphorylation cleavage assembly into polymeric proteins (> 1 polypeptide)
Posttranslational modifications of proteins do not include: peptide bond formation glycosylation acetylation of N-terminal peptide bond cleavage disulfide bond formation QUESTION 16 14 15 16 streptomycin puromycin 17 18 19 20 Which one of the following antibiotics does NOT function by interfering with the translational/post-translation process tunicamycin penicillin O tetracyclin O O
PLP is a cofactor for a number of enzymes involved in amino acid metabolism. Give an example of reaction in which PLP participates in cleavage of the a, b, and c bonds of an amino acid, as diagrammed in shown Fig.
The unfolding of the α helix of a polypeptide to a randomly coiled conformation is accompanied by a large decrease in a property called specific rotation, a measure of a solution’s capacity to rotate circularly polarized light. Polyglutamate, a polypeptide made up of only L-Gluresidues, has the α-helix conformation at pH 3. When the pH is raised to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (L-Lys residues) is an α helix at pH 10, but when the pH is lowered to 7 the specific rotation also decreases, as shown by the following graph. What is the explanation for the effect of the pH changes on the conformations of poly(Glu) and poly(Lys)? Why does the transition occur over such a narrow range of pH?
This image is showing the conformations of ubiquitin superimposed. What do the structures in this figure tell us about the dynamics of enzymes? Discuss the limitations of crystal structures in the analysis of proteins. What are the benefits? What are the advantages of NMR structures?
if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine proteases be affected? why? (assumin that the rest of the protein structure remain intact)
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)?