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Questions and Answers
Proteins and many other important biomolecules are made from nucleic acids.
False
Glycine is the only achiral member of the 20 common amino acids.
True
All amino acids exist as the L-optical form in Nature.
True
Amino acids contain only an acid, but not a base.
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Aromatic Amino Acids are crucial for the visualization of proteins.
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Oligopeptides contain 2-10 amino acids.
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Proteins generally contain between 50-400 residues.
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Peptide bonds have weak Resonance.
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A Tetrapeptide starts at the C-terminal AA.
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Cysteines can be linked via disulphide bonds.
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Glutathione contains Glu-Cys-Gly linked via sidechain Glu acid.
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Insulin is made from a single chain of amino acids.
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Polyacrylamide gel electrophoresis (PAGE) is used for the purification of DNA.
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Isoelectric points are not important for the characterization and separation of amino acids, peptides, and proteins.
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Short chains of AA are oligopeptides, and larger chains are known as polypeptides.
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Peptide linkages are the only way amino acids can be linked together to produce amides.
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Which type of amino acid is commonly found in nature?
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Which amino acid is the only achiral member of the 20 common amino acids?
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What type of linkages can cysteines form?
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Which book is recommended for the study of Amino Acids & Peptides?
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What is the characteristic of the isoelectric point for neutral amino acid side chains?
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Which suffix is used for oligopeptides containing 2-10 amino acids?
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What stabilizes peptide bonds by delocalization energy?
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What is the name of the tetrapeptide shown in the image?
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Which peptide is involved in pain control?
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How are cysteines linked in glutathione?
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What is insulin made from?
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What is used to denature proteins into uniform rods in polyacrylamide gel electrophoresis (PAGE)?
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What does the pH electrophoresis profile indicate?
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What does the term 'isolectric point' refer to?
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What do short chains of amino acids form when linked together by peptide bonds?
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What is the suffix used for polypeptides with between 10-50 residues?
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What is the characteristic of glycine among the 20 common amino acids?
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What type of amino acids are most commonly found in nature?
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What is the recommended book for the study of Amino Acids & Peptides?
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What is the only amino acid that exists as the L-optical form?
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What is the characteristic isoelectric point for neutral amino acid side chains?
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What type of bond can cysteines form?
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What is the name of the tetrapeptide: Alanylglutamylglycyllysine?
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What is the suffix used for oligopeptides containing 2-10 amino acids?
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What peptide is involved in pain control?
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What is the pH electrophoresis profile used to indicate?
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What is insulin made from?
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How are cysteines linked in glutathione?
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What do short chains of amino acids form when linked together by peptide bonds?
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What is the suffix used for polypeptides with between 10-50 residues?
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What stabilizes peptide bonds by delocalization energy?
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What is the name of the pentapeptide: Ser-Gly-Tyr-Ala-Leu?
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Study Notes
Proteins and Amino Acids
- Proteins are synthesized from nucleic acids, which encode the instructions for their formation.
- Glycine, the only achiral amino acid among the 20 common types, has no stereoisomer.
- All naturally occurring amino acids exist primarily in the L-optical form.
- Amino acids possess an acidic group and lack a basic group.
- Aromatic amino acids play a significant role in protein visualization due to their unique properties.
- Oligopeptides consist of 2 to 10 amino acids linked together.
- Proteins typically contain between 50 and 400 amino acid residues.
Peptide Bonds and Structures
- Peptide bonds exhibit weak resonance, contributing to their stability.
- A tetrapeptide is characterized by its four amino acid components, starting from the C-terminal amino acid.
- Cysteines can form disulfide bonds, which stabilize protein structure.
- Glutathione, an important tripeptide, is composed of glutamic acid, cysteine, and glycine, linked via the side chain of glutamic acid.
- Insulin is synthesized as a single chain of amino acids, indicating its polypeptide structure.
Techniques and Properties
- Polyacrylamide gel electrophoresis (PAGE) is utilized for DNA purification and analysis.
- Isoelectric points, while significant for certain applications, are deemed less critical for characterizing amino acids, peptides, and proteins.
- Short chains of amino acids linked by peptide bonds form oligopeptides, while longer chains are termed polypeptides.
Additional Key Points
- Cysteines in glutathione are linked through disulfide bonds, enhancing the molecule's stability.
- Various suffixes identify oligopeptides (2-10 residues) and polypeptides (generally 10-50 residues).
- The term "isoelectric point" signifies the pH at which an amino acid has no net charge, affecting its behavior in solutions.
- Glycine is distinctly recognized for its lack of chirality among common amino acids.
- Insulin, critical for glucose regulation, is formed from a specific sequence of amino acids.
- The profile in pH electrophoresis indicates the protein's charge and structure.
- The pentapeptide Ser-Gly-Tyr-Ala-Leu is a specific sequence that illustrates peptide bonding.
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Description
Test your knowledge of amino acids, peptides, and proteins in nature with this quiz based on the MPharm PHA111Amino Acids & Peptides lecture by Dr. Mark Gray. The quiz covers recommended readings and key concepts discussed in the lecture slides.
