The researcher isolated a small amount of guanidin from the synthesis reaction and analyzed its properties.

The researchers identified guanidine, a strong base with the formula HN=C(NH₂)₂ obtained by the oxidation of guanine, among the reaction products.

During the experiment, the team measured the pKa values of various guanidines to understand their protonation behavior.

The researchers observed that guanidins significantly increased the binding affinity of the peptide to its receptor.

Guanidinylation of the peptide increased its binding affinity to the receptor.

The lab report mistakenly listed guanidinum, which confused the students about the actual ion present.

During the synthesis, the guanidinyl unexpectedly rearranged to form a more stable amidine derivative.

During the experiment, the researchers observed that guanidinium stabilized the folded protein through specific electrostatic interactions.

The research group observed that guanidiniums stabilized the peptide's folded structure during the experiment.

To characterize its behavior, the chemist captured a transient guanidino and analyzed it by mass spectrometry.