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Questions and Answers
At what pKa value will glutamic acid primarily be found in its deprotonated form?
At what pKa value will glutamic acid primarily be found in its deprotonated form?
The side chain of lysine will be present as NH3+ at physiological pH.
The side chain of lysine will be present as NH3+ at physiological pH.
True
Which amino acid has a side chain pKa of 12.48?
Which amino acid has a side chain pKa of 12.48?
arginine
The pKa of the imidazole NH group is _____, indicating it is present as NH rather than NH2+.
The pKa of the imidazole NH group is _____, indicating it is present as NH rather than NH2+.
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Match the following amino acids with their side chain pKa values:
Match the following amino acids with their side chain pKa values:
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Which of the following elements is associated with the molybdenum cofactor in oxo transfer proteins?
Which of the following elements is associated with the molybdenum cofactor in oxo transfer proteins?
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The thioether of methionine is mentioned as a group associated with cobalt complex in vitamin B-12.
The thioether of methionine is mentioned as a group associated with cobalt complex in vitamin B-12.
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Which amino acids are mentioned as having carboxamide groups?
Which amino acids are mentioned as having carboxamide groups?
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The amino group of __________ is a group mentioned in the content.
The amino group of __________ is a group mentioned in the content.
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Match the following chemical groups with their associated amino acids:
Match the following chemical groups with their associated amino acids:
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Which amino acid has the abbreviation 'Cys'?
Which amino acid has the abbreviation 'Cys'?
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Arginine is one of the twenty common amino acids.
Arginine is one of the twenty common amino acids.
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What is the primary structure component of proteins?
What is the primary structure component of proteins?
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The pKa is a fundamental property of an acid, whereas pH is something we can adjust; when [HA] = [A−], it indicates that _____ equals pKa.
The pKa is a fundamental property of an acid, whereas pH is something we can adjust; when [HA] = [A−], it indicates that _____ equals pKa.
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Match the following amino acids with their abbreviations:
Match the following amino acids with their abbreviations:
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Which of the following amino acids has the highest molecular weight?
Which of the following amino acids has the highest molecular weight?
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The amino acid Glycine is represented by the letter 'G'.
The amino acid Glycine is represented by the letter 'G'.
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The amino acid with the side chain structure containing a thiol group is called _____ .
The amino acid with the side chain structure containing a thiol group is called _____ .
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Which of the following amino acids is NOT mentioned as a ligand in the context of metal-binding groups?
Which of the following amino acids is NOT mentioned as a ligand in the context of metal-binding groups?
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The iron complex of protoporphyrin IX is referred to as haem.
The iron complex of protoporphyrin IX is referred to as haem.
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Name one amino acid that functions as a ligand in metal-binding groups.
Name one amino acid that functions as a ligand in metal-binding groups.
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The ______ of histidine contains an imidazole group that acts as a ligand.
The ______ of histidine contains an imidazole group that acts as a ligand.
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Match the following ligands with their corresponding amino acids:
Match the following ligands with their corresponding amino acids:
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What role do metal-binding groups play in biology?
What role do metal-binding groups play in biology?
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Only carboxylates of aspartic acid serve as ligands in metal-binding groups.
Only carboxylates of aspartic acid serve as ligands in metal-binding groups.
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What is the chlorin ring associated with?
What is the chlorin ring associated with?
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Protoporphyrin IX is an important component of _____ complexes.
Protoporphyrin IX is an important component of _____ complexes.
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Which of the following ligands is derived from tyrosine?
Which of the following ligands is derived from tyrosine?
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What is the primary structure of a protein defined by?
What is the primary structure of a protein defined by?
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Hydrogen bonds play a significant role in determining the tertiary structure of proteins.
Hydrogen bonds play a significant role in determining the tertiary structure of proteins.
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What type of bond connects amino acids in a protein?
What type of bond connects amino acids in a protein?
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The secondary structure of proteins is characterized by __________ and __________.
The secondary structure of proteins is characterized by __________ and __________.
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Which of the following correctly describes secondary protein structure?
Which of the following correctly describes secondary protein structure?
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Match the type of protein structure to its description:
Match the type of protein structure to its description:
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Enterobactin is a type of peptide bond found in proteins.
Enterobactin is a type of peptide bond found in proteins.
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Name the bond that connects the carbonyl oxygen of one amino acid to the amino hydrogen of another.
Name the bond that connects the carbonyl oxygen of one amino acid to the amino hydrogen of another.
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What is the primary structure of the α-helix in proteins characterized by?
What is the primary structure of the α-helix in proteins characterized by?
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The R groups of amino acids in β-sheets alternate above and below the plane of the sheet.
The R groups of amino acids in β-sheets alternate above and below the plane of the sheet.
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How many amino acids are there in one complete turn of an α-helix?
How many amino acids are there in one complete turn of an α-helix?
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In β-sheets, the individual strands may be either __________ or __________.
In β-sheets, the individual strands may be either __________ or __________.
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Match each term with its description:
Match each term with its description:
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Which type of β-sheet configuration provides the strongest inter-strand stability?
Which type of β-sheet configuration provides the strongest inter-strand stability?
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The tertiary structure of proteins is primarily determined by the sequence of amino acids.
The tertiary structure of proteins is primarily determined by the sequence of amino acids.
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What type of bonding connects β-strands in a β-sheet?
What type of bonding connects β-strands in a β-sheet?
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Study Notes
Metals in Biochemistry/Biology
- Amino acids are the building blocks of proteins.
- See separate documents on Canvas for more details on amino acids and protein structures
- The Henderson-Hasselbalch equation helps predict the predominant form of an acid at a given pH.
- Acids have a pKa value, it is fundamental to the acid.
- pH is what can be adjusted
- pKa = pH + log [HA]/[A-]
- If pH < pKa, then [HA] > [A-], and the protonated form (HA) will be present.
- If pH > pKa, then [HA] < [A-], and the deprotonated form (A-) will be present.
Amino Acids
- There are twenty common amino acids.
- Each amino acid has a unique structure and properties.
- Amino acids are grouped by their properties.
- Examples of amino acids include Alanine, Arginine, Asparagine, etc.
- pKa values for the side chain groups of amino acids are often given in parentheses.
Protein Structures
- Proteins are made of amino acids connected by peptide bonds.
- The primary structure is the sequence of amino acids.
- The secondary structure describes the local folding of the polypeptide chain like α-helices and β-sheets.
- The tertiary structure is the overall 3D folding pattern of the entire polypeptide chain, determined by interactions between the R groups of the amino acids.
- The quaternary structure arises when multiple polypeptide chains assemble to form a larger functional unit.
- Examples include; Hemoglobin.
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Description
This quiz explores essential concepts of metals in biochemistry, focusing on amino acids, their structures, and the significance of pH in relation to pKa values. Understand how these factors influence the form of acids and the properties of amino acids. Test your knowledge on the building blocks of proteins and their functional roles.
