期刊
BIOPHYSICAL CHEMISTRY
卷 138, 期 3, 页码 115-119出版社
ELSEVIER
DOI: 10.1016/j.bpc.2008.09.011
关键词
Crystallization; Amino acids; Hydrophilicity/hydrophobicity; Sublimation; Polymorphism; Solvent-free
资金
- National Natural Science Foundation of China [20321303, 20590363]
This work studied the self-assembling (crystallizing) behaviour of amino acids in the absence of solvent and additives (by sublimation and deposition in vacuum), instead of from aqueous solution. It is found that the hydrophilicity/hydrophobicity of side-chains can significantly affect the crystallization of amino acids in the absence of solvent. Crystal structures of amino acids having hydrophobic side-chains (L.-valine, L-leucine, L-isoleucine and L-methionine) obtained from sublimation are the same with those obtained from aqueous solution. New polymorphs for six amino acids are thought to have been obtained, based on X-ray diffraction and IR data for three of them (L-tyrosine, L-Phyenylalanine and L-tryptophan), and just IR data for the other three (L-alanine, L-proline and L-threonine). (C) 2008 Elsevier B.V. All rights reserved.
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