The order of lithium ion affinities for the 20 common alpha-amino acids. Calculation of energy-well depth of ion-bound dinners

被引:10
作者
Andersen, UN [1 ]
Bojesen, G [1 ]
机构
[1] ODENSE UNIV,DEPT CHEM,DK-5230 ODENSE M,DENMARK
来源
JOURNAL OF THE CHEMICAL SOCIETY-PERKIN TRANSACTIONS 2 | 1997年 / 02期
关键词
D O I
10.1039/a604417d
中图分类号
O62 [有机化学];
学科分类号
070303 ; 081704 ;
摘要
In an earlier publication it was shown that the kinetic method for determination of proton affinities can be satisfactorily explained when the critical energies for decomposition of the proton-bound dimers are calculated from the Marcus equation. In this work it is shown that the critical energies for decomposition of alkali metal ion-bound dimers also seem to follow the Marcus equation. This supports the application of the kinetic method for measurements of alkali metal-ion affinities of organic molecules. Based on unimolecular decompositions of Li+-bound dimers, the order of lithium ion affinity of the common a-amino acids has been established as: Arg > His > Gin > Asn > Lys > Trp > Glu > Asp > Tyr > Met > Phe > Thr > Pro > Ser > Ile > Leu > Val > Cys > Ala > Gly.
引用
收藏
页码:323 / 327
页数:5
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