Biomolecules - Amino acids with Benzene Ring

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• Biomolecules are organic compounds that are essential for life.
• Amino acids are the building blocks of proteins.
• Amino acids are organic compounds containing both an amino group (-NH2) and a carboxyl group (-COOH).
• Amino acids with a benzene ring in their side chain are called aromatic amino acids.
• Examples of aromatic amino acids include phenylalanine, tyrosine, and tryptophan.

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Phenylalanine

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• Phenylalanine is one of the essential amino acids.
• It is classified as a nonpolar, hydrophobic amino acid.
• Molecular formula: C9H11NO2.
• Molecular weight: 165.19 g/mol.
• It contains a benzene ring as a side chain along with the amino and carboxyl groups.
• It is coded by the codons UUU and UUC.

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Tyrosine

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• Tyrosine is a semi-essential amino acid.
• It is classified as a polar, hydrophilic amino acid.
• Molecular formula: C9H11NO3.
• Molecular weight: 181.19 g/mol.
• It contains a hydroxyl group (-OH) attached to the benzene ring in addition to the amino and carboxyl groups.
• It is coded by the codons UAU and UAC.

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Tryptophan

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• Tryptophan is an essential amino acid.
• It is classified as a nonpolar, hydrophobic amino acid.
• Molecular formula: C11H12N2O2.
• Molecular weight: 204.23 g/mol.
• It contains an indole group (part of benzene ring) along with the amino and carboxyl groups.
• It is coded by the codons UGG.

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Properties of Aromatic Amino Acids

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• Aromatic amino acids have unique physical and chemical properties due to the presence of a benzene ring in their side chain.
• They are relatively hydrophobic due to the nonpolar nature of the benzene ring.
• They tend to have bulky side chains, which can affect protein structure and function.
• These amino acids play important roles in protein folding and stabilization.
• They often participate in specific protein-protein interactions.

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Function of Aromatic Amino Acids

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• Aromatic amino acids play crucial roles in protein structure and function.
• They are involved in protein folding and stabilization.
• They contribute to the hydrophobic core of proteins, promoting stability.
• They participate in ligand binding sites and can interact with other molecules through their aromatic rings.
• Aromatic amino acids are also important in various physiological processes, such as neurotransmitter synthesis.

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Phenylalanine Example

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• Phenylalanine is involved in the synthesis of various neurotransmitters, including dopamine and norepinephrine.
• It is an essential amino acid, which means it must be obtained through the diet.
• Phenylalanine is a precursor for the biosynthesis of tyrosine, another aromatic amino acid.
• It is also used in the production of various drugs and food additives.
• An example of a drug derived from phenylalanine is L-DOPA, used for the treatment of Parkinson’s disease.

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Tyrosine Example

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• Tyrosine is involved in the synthesis of important molecules, such as thyroid hormones.
• It plays a crucial role in the production of melanin, the pigment responsible for skin and hair color.
• Tyrosine is also a precursor for the synthesis of important neurotransmitters, including dopamine and epinephrine.
• It is commonly used as a supplement in various forms due to its potential health benefits.
• Tyrosine can be found naturally in various foods, including dairy products, meat, fish, and legumes.

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Tryptophan Example

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• Tryptophan is a precursor for the synthesis of serotonin, a neurotransmitter involved in mood regulation and sleep.
• It is an essential amino acid that needs to be obtained through the diet.
• Tryptophan-rich foods include turkey, chicken, nuts, seeds, and dairy products.
• Tryptophan supplements are sometimes used to promote healthy sleep and improve mood.
• It is also a precursor for the synthesis of niacin, a B vitamin essential for various cellular processes.

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Summary

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• Aromatic amino acids with benzene rings in their side chain include phenylalanine, tyrosine, and tryptophan.
• These amino acids play important roles in protein structure, function, and various physiological processes.
• Their unique properties contribute to protein folding, stability, ligand binding, and protein-protein interactions.
• Understanding the properties and functions of aromatic amino acids is crucial for studying biomolecules and their role in life processes.

Slide 11

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• Aromatic amino acids have unique physical and chemical properties
• Due to the presence of a benzene ring in their side chain
• Relatively hydrophobic due to the nonpolar nature of the benzene ring
• Bulky side chains can affect protein structure and function
• Play important roles in protein folding and stabilization

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Slide 12

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• Aromatic amino acids participate in specific protein-protein interactions
• They often form binding sites for other molecules
• Can interact with ligands through their aromatic rings
• Provide stability and contribute to the hydrophobic core of proteins
• Examples include phenylalanine, tyrosine, and tryptophan

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Slide 13

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• Phenylalanine is an essential amino acid
• Coded by the codons UUU and UUC
• Molecular formula: C9H11NO2
• Molecular weight: 165.19 g/mol
• Nonpolar, hydrophobic amino acid

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Slide 14

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• Phenylalanine is a precursor for the biosynthesis of tyrosine
• Involved in the synthesis of neurotransmitters dopamine and norepinephrine
• Used in the production of drugs and food additives
• Example: L-DOPA for Parkinson’s disease treatment
• Must be obtained through the diet

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Slide 15

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• Tyrosine is a semi-essential amino acid
• Coded by the codons UAU and UAC
• Molecular formula: C9H11NO3
• Molecular weight: 181.19 g/mol
• Polar, hydrophilic amino acid

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Slide 16

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• Tyrosine is involved in the production of thyroid hormones
• Crucial for the synthesis of melanin, the pigment responsible for skin and hair color
• Precursor for the synthesis of neurotransmitters dopamine and epinephrine
• Used as a supplement and found naturally in various foods
• Important for various cellular processes

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Slide 17

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• Tryptophan is an essential amino acid
• Coded by the codon UGG
• Molecular formula: C11H12N2O2
• Molecular weight: 204.23 g/mol
• Nonpolar, hydrophobic amino acid

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Slide 18

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• Tryptophan is a precursor for the synthesis of serotonin
• Neurotransmitter involved in mood regulation and sleep
• Must be obtained through the diet
• Found in foods such as turkey, chicken, nuts, seeds, and dairy products
• Used as a supplement for healthy sleep and improved mood

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Slide 19

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• Tryptophan is also a precursor for the synthesis of niacin
• Niacin is a B vitamin essential for various cellular processes
• Tryptophan-rich foods are important sources of niacin
• Examples include turkey, chicken, nuts, and dairy products
• Tryptophan supplements can provide additional niacin

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Slide 20

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• Understanding the properties and functions of aromatic amino acids is essential in studying biomolecules
• Aromatic amino acids contribute to protein structure, stability, and ligand binding
• Phenylalanine, tyrosine, and tryptophan are examples of aromatic amino acids with benzene rings in their side chains
• These amino acids play crucial roles in protein folding, stabilization, and various physiological processes
• Mastery of these concepts is important for success in the 12th Boards examination in chemistry.

21. Functions of Aromatic Amino Acids

• Aromatic amino acids play crucial roles in protein structure and function.
• They contribute to the hydrophobic core of proteins, promoting stability.
• They participate in ligand binding sites and can interact with other molecules through their aromatic rings.
• Examples include phenylalanine, tyrosine, and tryptophan.
• Aromatic amino acids are also important in various physiological processes, such as neurotransmitter synthesis.

22. Phenylalanine Example

• Phenylalanine is involved in the synthesis of various neurotransmitters, including dopamine and norepinephrine.
• It is an essential amino acid, which means it must be obtained through the diet.
• Phenylalanine is a precursor for the biosynthesis of tyrosine, another aromatic amino acid.
• It is also used in the production of various drugs and food additives.
• An example of a drug derived from phenylalanine is L-DOPA, used for the treatment of Parkinson’s disease.

23. Tyrosine Example

• Tyrosine is involved in the synthesis of important molecules, such as thyroid hormones.
• It plays a crucial role in the production of melanin, the pigment responsible for skin and hair color.
• Tyrosine is also a precursor for the synthesis of important neurotransmitters, including dopamine and epinephrine.
• It is commonly used as a supplement in various forms due to its potential health benefits.
• Tyrosine can be found naturally in various foods, including dairy products, meat, fish, and legumes.

24. Tryptophan Example

• Tryptophan is a precursor for the synthesis of serotonin, a neurotransmitter involved in mood regulation and sleep.
• It is an essential amino acid that needs to be obtained through the diet.
• Tryptophan-rich foods include turkey, chicken, nuts, seeds, and dairy products.
• Tryptophan supplements are sometimes used to promote healthy sleep and improve mood.
• It is also a precursor for the synthesis of niacin, a B vitamin essential for various cellular processes.

25. Properties of Aromatic Amino Acids

• Aromatic amino acids have unique physical and chemical properties.
• The presence of a benzene ring in their side chain gives them their characteristic properties.
• They are relatively hydrophobic due to the nonpolar nature of the benzene ring.
• Aromatic amino acids often have bulky side chains, which can affect protein structure and function.
• These amino acids play important roles in protein folding and stabilization.

26. Protein Structure

• Proteins have a hierarchical structure.
• Primary structure refers to the sequence of amino acids in a protein.
• Secondary structure refers to local spatial arrangements of the polypeptide chain, including α-helices and β-sheets.
• Tertiary structure refers to the overall 3D structure of a protein.
• Quaternary structure refers to the interactions between multiple protein subunits.

27. Protein Folding

• Protein folding refers to the process by which an unfolded polypeptide chain adopts its functional 3D conformation.
• Folding is governed by the interactions between amino acid side chains and the surrounding environment.
• Various factors, such as temperature, pH, and presence of chaperone proteins, can influence folding.
• Misfolding of proteins can lead to diseases such as Alzheimer’s and Parkinson’s.
• Understanding protein folding is crucial for understanding protein structure and function.

28. Protein Stability

• Protein stability refers to the tendency of a protein to maintain its native conformation.
• Stability is influenced by various factors, including hydrogen bonding, hydrophobic interactions, and electrostatic interactions.
• Denaturation, which involves the disruption of the protein’s secondary, tertiary, and quaternary structure, can lead to loss of protein function.
• Factors such as temperature, pH, and chemical denaturants can influence protein stability.
• Maintaining protein stability is essential for proper cellular function.

29. Protein-Ligand Interactions

• Proteins can interact with various molecules, known as ligands.
• Ligands can bind to specific binding sites on proteins, leading to conformational changes and functional effects.
• Aromatic amino acids in proteins often contribute to ligand binding sites due to their ability to interact with ligand molecules through their aromatic rings.
• Examples of ligand-protein interactions include enzyme-substrate interactions and receptor-ligand interactions.
• Understanding protein-ligand interactions is important for drug design and understanding disease mechanisms.

30. Conclusion

• Aromatic amino acids with benzene rings in their side chains play important roles in protein structure and function.
• Phenylalanine, tyrosine, and tryptophan are examples of aromatic amino acids.
• These amino acids contribute to protein folding, stability, ligand binding, and protein-protein interactions.
• Understanding the properties and functions of aromatic amino acids is crucial for studying biomolecules and their role in life processes.
• Mastery of these concepts is important for success in the 12th Boards examination in chemistry.