Specific ion binding to nonpolar surface patches of proteins
(2008) In Journal of the American Chemical Society 130(35). p.3-11582- Abstract
- Employing detailed atomistic modeling we study the mechanisms behind ion binding to proteins and other biomolecules and conclude that (1) small, hard ions bind via direct ion pairing to charged surface groups and (2) large, soft ions bind to nonpolar groups via a solvent assisted attraction. Our predictions are in qualitative agreement with bulk solution data and may provide an important clue for the basic understanding of ion-specific effects in biological systems.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/7763555
- author
- Lund, Mikael LU ; Vrbka, Lubos and Jungwirth, Pavel
- organization
- publishing date
- 2008
- type
- Contribution to specialist publication or newspaper
- publication status
- published
- subject
- keywords
- Ions, Ions: chemistry, Models, Molecular, Muramidase, Muramidase: chemistry, Potassium Chloride, Muramidase: metabolism, Potassium Iodide, Potassium Chloride: chemistry, Potassium Iodide: chemistry, Protein Binding, Surface Properties, Water: chemistry, Water
- in
- Journal of the American Chemical Society
- volume
- 130
- issue
- 35
- pages
- 3 - 11582
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- scopus:51349165268
- pmid:18686949
- ISSN
- 1520-5126
- DOI
- 10.1021/ja803274p
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 57cf5bee-d4eb-4a16-8619-b171a8a4d40b (old id 7763555)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/18686949
- date added to LUP
- 2016-04-01 13:57:17
- date last changed
- 2023-01-04 01:50:41
@misc{57cf5bee-d4eb-4a16-8619-b171a8a4d40b, abstract = {{Employing detailed atomistic modeling we study the mechanisms behind ion binding to proteins and other biomolecules and conclude that (1) small, hard ions bind via direct ion pairing to charged surface groups and (2) large, soft ions bind to nonpolar groups via a solvent assisted attraction. Our predictions are in qualitative agreement with bulk solution data and may provide an important clue for the basic understanding of ion-specific effects in biological systems.}}, author = {{Lund, Mikael and Vrbka, Lubos and Jungwirth, Pavel}}, issn = {{1520-5126}}, keywords = {{Ions; Ions: chemistry; Models; Molecular; Muramidase; Muramidase: chemistry; Potassium Chloride; Muramidase: metabolism; Potassium Iodide; Potassium Chloride: chemistry; Potassium Iodide: chemistry; Protein Binding; Surface Properties; Water: chemistry; Water}}, language = {{eng}}, number = {{35}}, pages = {{3--11582}}, publisher = {{The American Chemical Society (ACS)}}, series = {{Journal of the American Chemical Society}}, title = {{Specific ion binding to nonpolar surface patches of proteins}}, url = {{http://dx.doi.org/10.1021/ja803274p}}, doi = {{10.1021/ja803274p}}, volume = {{130}}, year = {{2008}}, }