Premium
Molecular dynamics and NMR studies of proteins in ionic solutions
Author(s) -
Baianu I. C.,
Kumosinski T. F.,
Wei T. C.
Publication year - 1999
Publication title -
macromolecular symposia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.257
H-Index - 76
eISSN - 1521-3900
pISSN - 1022-1360
DOI - 10.1002/masy.19991400123
Subject(s) - chemistry , aqueous solution , electrolyte , molecular dynamics , relaxation (psychology) , ionic bonding , ion , cationic polymerization , amide , salt (chemistry) , chemical physics , inorganic chemistry , computational chemistry , organic chemistry , psychology , social psychology , electrode
The molecular dynamics of water and selected ions was studied in concentrated electrolyte solutions with, or without, proteins added. Our experimental results by multinuclear spin relaxation techniques were then compared with molecular dynamics computations for water and ions in concentrated electrolyte solutions. The mechanisms for the anionic and cationic interactions with myofibrillar proteins in aqueous solutions were investigated by nuclear magnetic resonance over a wide range of salt concentrations. The multinuclear spin relaxation data were analyzed with a thermodynamic linkage model of hydrated ion clusters of various sizes and composition. Protein amide groups were found to bind to anions with strengths in the order of the lyotropic series.