@article{oai:kanazawa-u.repo.nii.ac.jp:00007723,
 author = {Ohta, Akio and Ozawa, Noriaki and Nakashima, Satoru and Asakuwa, Tsuyoshi and Miyagishi, Shigeyoshi},
 issue = {4},
 journal = {Colloid and Polymer Science},
 month = {Apr},
 note = {The Krafft temperatures and the enthalpies of solution of six kinds of N-hexadecanoyl amino acid surfactant (Gly, Ala, Val, Leu, Ile, and Phe) were obtained from both solubility measurements and differential scanning calorimetry. It was shown that the Krafft temperature of N-hexadecanoyl amino acid surfactant increased with decreasing size of the amino acid residue except for the case of phenylalanine. On the other hand, the enthalpy of solution was endothermic and increased with decreasing size of the amino acid residue except for the cases of glycine and phenylalanine. It was found from these results that the D-L interaction was superior to the L-L interaction in solid state of N-hexadecanoyl amino acid surfactant salt for both the alanine and phenylalanine systems. It was suggested by ab initio calculations that the difference of the magnitude of the peptide-peptide hydrogen bonding was the dominant factor for the chiral effect., 金沢大学工学部},
 pages = {363--369},
 title = {Krafft temperature and enthalpy of solution of N-acyl amino acid surfactants and their racemic modifications: Effect of the amino acid residue},
 volume = {281},
 year = {2003}
}