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Multiple Choice
Ligation of a ubiquitin peptide's ______________ charged carboxylate group to the R-group of a target protein's ___________ residue forms a(n) _____________ bond.
A
Neutrally ; Histidine ; Hydrogen.
B
Negatively ; Leucine ; Isopeptide.
C
Positively ; Lysine ; Ionic.
D
Positively ; Lysine ; Disulfide.
E
Negatively; Lysine ; Hydrogen.
F
Negatively ; Lysine ; Isopeptide.
Verified step by step guidance
1
Understand the process of ubiquitination: Ubiquitination involves attaching a ubiquitin molecule to a substrate protein, which is crucial for protein degradation and regulation.
Identify the chemical groups involved: The ubiquitin peptide has a carboxylate group, which is negatively charged. This is important for forming a bond with the target protein.
Determine the target residue: The target protein's residue that participates in ubiquitination is typically a lysine. Lysine has an amino group in its side chain, which can form a bond with the carboxylate group.
Recognize the type of bond formed: The bond formed between the carboxylate group of ubiquitin and the amino group of lysine is an isopeptide bond. This is a type of covalent bond that is crucial for the stability of the ubiquitin-protein complex.
Review the options: Match the characteristics of the ubiquitination process with the given options. The correct choice is 'Negatively ; Lysine ; Isopeptide', as it accurately describes the charge of the carboxylate group, the target residue, and the type of bond formed.