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Questions and Answers
What functional groups are present in amino acids?
What functional groups are present in amino acids?
What determines the optical isomerism of amino acids?
What determines the optical isomerism of amino acids?
How are L- and D-amino acids classified based on their structure?
How are L- and D-amino acids classified based on their structure?
In what form do amino acids mostly exist in biological systems?
In what form do amino acids mostly exist in biological systems?
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Which carbon atom in an amino acid exhibits asymmetric behavior?
Which carbon atom in an amino acid exhibits asymmetric behavior?
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All amino acids, except glycine, have four distinct groups held by the α-carbon
All amino acids, except glycine, have four distinct groups held by the α-carbon
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Optical isomers of amino acids are determined by the configuration of L- and D-glyceraldehyde
Optical isomers of amino acids are determined by the configuration of L- and D-glyceraldehyde
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The proteins are composed of D-α-amino acids
The proteins are composed of D-α-amino acids
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Amino acids do not exhibit optical isomerism
Amino acids do not exhibit optical isomerism
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The carboxyl group of amino acids is basic in nature
The carboxyl group of amino acids is basic in nature
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Is selenocysteine a 21st amino acid containing the trace element selenium in place of the sulfur atom of cysteine?
Is selenocysteine a 21st amino acid containing the trace element selenium in place of the sulfur atom of cysteine?
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Selenocysteine occurs at the active sites of several enzymes that catalyze redox reactions.
Selenocysteine occurs at the active sites of several enzymes that catalyze redox reactions.
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Selenocysteine is inserted directly into a growing polypeptide during translation.
Selenocysteine is inserted directly into a growing polypeptide during translation.
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Posttranslational modifications of amino acids can generate novel R-groups that impart further properties.
Posttranslational modifications of amino acids can generate novel R-groups that impart further properties.
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The carboxylation of glutamyl residues of proteins of the coagulation cascade to γ-carboxyglutamyl residues forms a chelating group for the calcium ion essential for blood coagulation.
The carboxylation of glutamyl residues of proteins of the coagulation cascade to γ-carboxyglutamyl residues forms a chelating group for the calcium ion essential for blood coagulation.
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