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Dissecting Hofmeister Effects: Direct Anion–Amide Interactions Are Weaker than Cation–Amide Binding
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2016-05-30 , DOI: 10.1002/anie.201602769 Vasileios Balos 1 , Heejae Kim 1 , Mischa Bonn 1 , Johannes Hunger 1
Angewandte Chemie International Edition ( IF 16.1 ) Pub Date : 2016-05-30 , DOI: 10.1002/anie.201602769 Vasileios Balos 1 , Heejae Kim 1 , Mischa Bonn 1 , Johannes Hunger 1
Affiliation
Whereas there is increasing evidence for ion‐induced protein destabilization through direct ion–protein interactions, the strength of the binding of anions to proteins relative to cation–protein binding has remained elusive. In this work, the rotational mobility of a model amide in aqueous solution was used as a reporter for the interactions of different anions with the amide group. Protein‐stabilizing salts such as KCl and KNO3 do not affect the rotational mobility of the amide. Conversely, protein denaturants such as KSCN and KI markedly reduce the orientational freedom of the amide group. Thus these results provide evidence for a direct denaturation mechanism through ion–protein interactions. Comparing the present findings with results for cations shows that in contrast to common belief, anion–amide binding is weaker than cation–amide binding.
中文翻译:
剖析Hofmeister效应:直接的阴离子-酰胺相互作用比阳离子-酰胺键更弱
尽管有越来越多的证据表明通过直接的离子-蛋白质相互作用,离子诱导的蛋白质不稳定,但相对于阳离子-蛋白质结合,阴离子与蛋白质的结合强度仍然难以捉摸。在这项工作中,模型酰胺在水溶液中的旋转迁移率用作不同阴离子与酰胺基团相互作用的报告分子。蛋白质稳定盐,例如KCl和KNO 3不影响酰胺的旋转迁移率。相反,蛋白质变性剂(例如KSCN和KI)显着降低了酰胺基团的取向自由度。因此,这些结果为通过离子-蛋白质相互作用的直接变性机理提供了证据。将目前的发现与阳离子的结果进行比较表明,与通常的看法相反,阴离子-酰胺的结合力弱于阳离子-酰胺的结合力。
更新日期:2016-05-30
中文翻译:
剖析Hofmeister效应:直接的阴离子-酰胺相互作用比阳离子-酰胺键更弱
尽管有越来越多的证据表明通过直接的离子-蛋白质相互作用,离子诱导的蛋白质不稳定,但相对于阳离子-蛋白质结合,阴离子与蛋白质的结合强度仍然难以捉摸。在这项工作中,模型酰胺在水溶液中的旋转迁移率用作不同阴离子与酰胺基团相互作用的报告分子。蛋白质稳定盐,例如KCl和KNO 3不影响酰胺的旋转迁移率。相反,蛋白质变性剂(例如KSCN和KI)显着降低了酰胺基团的取向自由度。因此,这些结果为通过离子-蛋白质相互作用的直接变性机理提供了证据。将目前的发现与阳离子的结果进行比较表明,与通常的看法相反,阴离子-酰胺的结合力弱于阳离子-酰胺的结合力。