General, Organic, and Biological Chemistry
General, Organic, and Biological Chemistry
7th Edition
ISBN: 9781285853918
Author: H. Stephen Stoker
Publisher: Cengage Learning
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Concept explainers

Neutral Amino Acids
Amino acids which do not have any charge on them are neutral amino acids.
Globular Protein
The globular proteins refer to the shape of protein specifically spherical in nature apart from spherical form fibrous, disordered and membrane-bound proteins exist. These globular proteins are miscible in water and form a colloidal solution rather than …
Dimer
Dimers are basic organic compounds, which are derivates of oligomers. It is formed by the combination of two monomers which could potentially be strong or weak and in most cases covalent or intermolecular in nature. Identical monomers are called homodime…
Dipeptide
A dipeptide is considered a mixture of two distinct amino acids. Since the amino acids are distinct, based on their composition, two dipeptide's isomers can be produced. Various dipeptides are biologically essential and are therefore crucial to industry.
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**Chemical Compound Visualization and Editing** The image above displays two chemical compound structures with an option for editing. Each compound is framed within a green dashed box, and a green checkmark in the upper right corner indicates verification or correctness. **Top Compound:** 1. The first structure is a phenylalanine molecule. It consists of a benzene ring (a hexagon) attached to a two-carbon chain. The carbon chain is bonded to an amine group (NH3+) and a carboxylate group (COO-). 2. Below this structure, there is a blue button labeled "edit structure...," suggesting that users can click this button to make modifications to the chemical structure. **Bottom Compound:** 1. The second structure represents a methionine molecule. It includes a backbone similar to phenylalanine but has a sulfur atom incorporated into its side chain. The structure shows a carboxyl group (COO-), an amine group (NH3+), and a sulfur atom attached to the side chain. 2. This structure also has a blue button labeled "edit structure...," indicating that it can be edited as well. These visual representations emphasize the importance of molecular structure editing and provide users with an interactive element to enhance their understanding of organic chemistry. By interacting with the "edit structure..." buttons, users can alter the chemical structures, allowing for a hands-on learning experience in molecular chemistry.
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Transcribed Image Text:**Chemical Compound Visualization and Editing** The image above displays two chemical compound structures with an option for editing. Each compound is framed within a green dashed box, and a green checkmark in the upper right corner indicates verification or correctness. **Top Compound:** 1. The first structure is a phenylalanine molecule. It consists of a benzene ring (a hexagon) attached to a two-carbon chain. The carbon chain is bonded to an amine group (NH3+) and a carboxylate group (COO-). 2. Below this structure, there is a blue button labeled "edit structure...," suggesting that users can click this button to make modifications to the chemical structure. **Bottom Compound:** 1. The second structure represents a methionine molecule. It includes a backbone similar to phenylalanine but has a sulfur atom incorporated into its side chain. The structure shows a carboxyl group (COO-), an amine group (NH3+), and a sulfur atom attached to the side chain. 2. This structure also has a blue button labeled "edit structure...," indicating that it can be edited as well. These visual representations emphasize the importance of molecular structure editing and provide users with an interactive element to enhance their understanding of organic chemistry. By interacting with the "edit structure..." buttons, users can alter the chemical structures, allowing for a hands-on learning experience in molecular chemistry.
**Hydrolysis of a Tripeptide** **Instruction:** Draw the structures of the amino acids formed when the tripeptide below is hydrolyzed. **Tripeptide Structure:** The chemical structure of the tripeptide is presented. It consists of three amino acid residues connected via peptide bonds. - The leftmost residue is valine (Val) with the side chain isopropyl group (CH(CH₃)₂). - The middle residue is tyrosine (Tyr) with a benzene ring bearing a hydroxyl group (OH). - The rightmost residue is methionine (Met) with a side chain containing a thioether group (CH₂CH₂SCH₃). **Diagram Explanation:** An arrow indicates the next step, depicting the hydrolysis of the tripeptide to yield individual amino acids. **Hydrolyzed Components:** The lower structure, shown in red, represents one of the peptides resulting from the hydrolysis process. This specific peptide has the following structure: - A central carbon (alpha carbon) bonded to an amino group (NH₃⁺). - A carboxyl group (COO⁻). - A side chain specific to one of the amino acids from the original tripeptide. The exact structure illustrated below the arrow is the alpha-amino acid with its side chain intact as the tripeptide splits into its constituent amino acids. **Edit Prompt:** - The image includes an editable structure button labeled “edit structure ...” indicating that the viewer can interact with the structure for educational purposes. **Key Learning Points:** - Understanding peptide bond formation and hydrolysis. - Recognizing the structure of amino acids. - Ability to translate chemical structures into their corresponding amino acids. This exercise helps students learn how to identify specific amino acids resulting from enzymatic or chemical hydrolysis of peptides, a fundamental concept in biochemistry.
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Transcribed Image Text:**Hydrolysis of a Tripeptide** **Instruction:** Draw the structures of the amino acids formed when the tripeptide below is hydrolyzed. **Tripeptide Structure:** The chemical structure of the tripeptide is presented. It consists of three amino acid residues connected via peptide bonds. - The leftmost residue is valine (Val) with the side chain isopropyl group (CH(CH₃)₂). - The middle residue is tyrosine (Tyr) with a benzene ring bearing a hydroxyl group (OH). - The rightmost residue is methionine (Met) with a side chain containing a thioether group (CH₂CH₂SCH₃). **Diagram Explanation:** An arrow indicates the next step, depicting the hydrolysis of the tripeptide to yield individual amino acids. **Hydrolyzed Components:** The lower structure, shown in red, represents one of the peptides resulting from the hydrolysis process. This specific peptide has the following structure: - A central carbon (alpha carbon) bonded to an amino group (NH₃⁺). - A carboxyl group (COO⁻). - A side chain specific to one of the amino acids from the original tripeptide. The exact structure illustrated below the arrow is the alpha-amino acid with its side chain intact as the tripeptide splits into its constituent amino acids. **Edit Prompt:** - The image includes an editable structure button labeled “edit structure ...” indicating that the viewer can interact with the structure for educational purposes. **Key Learning Points:** - Understanding peptide bond formation and hydrolysis. - Recognizing the structure of amino acids. - Ability to translate chemical structures into their corresponding amino acids. This exercise helps students learn how to identify specific amino acids resulting from enzymatic or chemical hydrolysis of peptides, a fundamental concept in biochemistry.
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