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Influence of a Hydrophobic Environment on the Structure of Arginine‐Carboxylate Salt Bridge
Author(s) -
Feng Yong,
Liu Lei,
Mu TingWei,
Guo QingXiang
Publication year - 2002
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.20020201007
Subject(s) - salt bridge , chemistry , carboxylate , salt (chemistry) , arginine , bridge (graph theory) , hydrophobic effect , polymer chemistry , amino acid , stereochemistry , organic chemistry , biochemistry , medicine , mutant , gene
The exact structure of an arginine‐carboxylate salt bridge in different chemical environments remains a controversial problem. In the present work, the zwitterionic and neutral forms of arginine‐carboxylate salt bridge were studied by the B3LYP/6‐311G (d, p)//PM3 method. It turns out that the neutral forms are more stable than the zwitterionic counterparts in gas phase. However, when bound by α‐cyclodextrin, the zwitterionic forms become more stable than the corresponding neutral ones. It is suggested that the hydrophobic environment provided by the cydodextrin cavity leads to such behavior. Therefore, the salt bridge still could be in a zwitterionic form in the hydrophobic interior of the real proteins.