Final answer:
The amino acids leucine, histidine, and arginine are eluted in order based on their polarity and charge, with leucine (a nonpolar amino acid) eluting first, followed by histidine, then arginine (both basic but with different affinities for their positive charge).
Step-by-step explanation:
The question is asking in what order the amino acids arginine (Arg), histidine (His), and leucine (Leu) are eluted during a chromatography process. Considering the properties of these amino acids, we know that basic amino acids like arginine and histidine, which contain a positive charge, are eluted after neutral or nonpolar amino acids like leucine. Therefore, leucine, which is part of Group 1 and not positively charged, will elute first due to its more hydrophobic nature, followed by the basic amino acids. Among the basic amino acids, histidine, which has a weaker affinity for the positive charge, is usually eluted before arginine which has a strong positive charge. Thus, the order of elution is: Leu, His, Arg.
The elution order of amino acids in chromatography is influenced by their chemical properties. In ion-exchange chromatography, for example, amino acids are separated based on their charges.
Without specific information about the conditions of the chromatography (e.g., the type of chromatography, the elution buffer used, etc.), it's challenging to determine the exact elution order.
However, if we assume a hypothetical order based on the general properties of the amino acids:
Leu, His, Arg
This is a speculative answer, and the actual elution order would depend on the specific conditions of the chromatography experiment.