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Where is the linkage made that combines two amino acids? a. between the \(\mathrm{R}\) group of one amino acid and the R group of the second b. between the carboxyl group of one amino acid and the amino group of the other c. between the 6 carbon of both amino acids d. between the nitrogen atoms of the amino groups \(\quad\) in the amino acids

Short Answer

Expert verified
The linkage is made between the carboxyl group of one amino acid and the amino group of the other (option b).

Step by step solution

01

Identify the Functional Groups Involved in Peptide Bond Formation

A peptide bond is formed between the amino group (-NH2) of one amino acid and the carboxyl group (-COOH) of another amino acid.
02

Understanding the Peptide Bond

In a peptide bond, a molecule of water is released in a dehydration synthesis reaction.
03

Examine the Options Given

Option a discusses the R groups, option b the carboxyl and amino groups, option c the carbon atoms, and option d the nitrogen atoms.
04

Select the Correct Answer

Considering peptide bonds involve the carboxyl group of one amino acid and the amino group of the other, the correct answer is b.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

Amino Acids
Amino acids are the building blocks of proteins. Each amino acid has a central carbon atom (α-carbon) attached to four different groups: a hydrogen atom, an amino group (-NH2), a carboxyl group (-COOH), and a unique side chain (R group). This side chain, or R group, determines the properties and function of each amino acid.
There are 20 different standard amino acids found in proteins. These can be classified based on the characteristics of their side chains as nonpolar, polar, acidic, or basic.
Understanding amino acids is crucial since they play roles in various processes, such as protein synthesis, enzymatic reactions, and cellular signaling.
  • Central carbon (α-carbon): The central atom of the amino acid structure.
  • Amino group (-NH2): A functional group that acts as a base by accepting hydrogen ions.
  • Carboxyl group (-COOH): A functional group that acts as an acid by donating hydrogen ions.
  • R group: The variable group that defines the distinct characteristics of each amino acid.
A solid foundation in amino acid structure and properties helps in understanding more complex concepts like peptide bond formation and protein structure.
Dehydration Synthesis
Dehydration synthesis, also known as a condensation reaction, is the process by which monomers combine to form polymers, releasing a molecule of water in the process. In the context of amino acids, dehydration synthesis is the key reaction involved in forming peptide bonds.
When two amino acids come together, the carboxyl group of one amino acid reacts with the amino group of another. During this reaction:
  • A hydroxyl group (-OH) from the carboxyl group of one amino acid and a hydrogen atom (H) from the amino group of the other amino acid are removed.
  • This removal results in the formation of a water molecule (H2O).
  • The remaining atoms are joined together by a covalent bond known as a peptide bond.
This entire mechanism is facilitated by enzymes in living organisms. Dehydration synthesis is how dipeptides (two amino acids linked by a peptide bond), polypeptides (long chains of amino acids), and ultimately proteins are formed.
The understanding of dehydration synthesis is not only important for peptide bond formation but also for the synthesis of other biological macromolecules such as nucleic acids and polysaccharides.
Functional Groups in Peptides
Functional groups are specific groupings of atoms within molecules that have their own characteristic properties. In peptides and proteins, the primary functional groups involved in peptide bond formation are the amino and carboxyl groups.
A peptide bond forms when:
  • The carboxyl group (-COOH) of one amino acid reacts with the amino group (-NH2) of another amino acid during dehydration synthesis.
  • This reaction releases a molecule of water and creates a covalent bond between the carbon atom of the carboxyl group and the nitrogen atom of the amino group.
Peptide bonds are quite strong and rigid, providing stability to the protein structure. Additionally, the R groups (side chains) of the amino acids are crucial as they affect the folding and function of the protein. They can be polar, nonpolar, acidic, or basic, which impacts how the protein interacts with its environment and other molecules.
To summarize, the functional groups are crucial in determining the structure and function of peptides and proteins. The amino (-NH2) and carboxyl (-COOH) groups directly participate in forming the peptide bonds, while the R group influences the protein's overall shape and properties.

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Most popular questions from this chapter

Which type of body cell would have a higher amount of cholesterol in its membrane? a. a cartilage cell b. a liver cell c. a red blood cell d. a spleen cell

Which structural level of proteins is most often associated with their biological function? a. the primary structure b. the secondary structure c. the tertiary structure d. the quaternary structure

Which of the following characteristics is not true for saturated fats? a. They are solid at room temperature. b. They have single bonds within the carbon chain. c. They tend to dissolve in water easily.

Dehydration synthesis leads to the formation of what? a. monomers b. polymers c. carbohydrates only d. water only

For many years, scientist believed that proteins were the source of heritable information. There are many thousands of different proteins in a cell, and they mediate the cell's metabolism, producing the traits and characteristics of a species. Researchers working with DNA viruses proved that it is DNA that stores and passes on genes. They worked with viruses with an outer coat of protein and a DNA strand inside. How did they prove that it was DNA, not protein, which is the primary source of heritable information? a. The DNA and protein of the virus were tagged with different isotopes and exposed to host cell where only the DNA was transferred to the host. b. The DNA was tagged with an isotope, which was retained in the virus, proving it to be the genetic material. c. The viral protein was tagged with an isotope, and the host cell was infected by it. This protein was transferred to the host. d. The viral DNA, when sequenced, was found to be present in the host cell proving it to be the hereditary material instead of protein.

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