Document Detail


Studying Ion Exchange in Solution and at Biological Membranes by FCS.
MedLine Citation:
PMID:  23280113     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
By FCS, a wide range of processes can be studied, covering time ranges from subnanoseconds to seconds. In principle, any process at equilibrium conditions can be measured, which reflects itself by a change in the detected fluorescence intensity. In this review, it is described how FCS and variants thereof can be used to monitor ion exchange, in solution and along biological membranes. Analyzing fluorescence fluctuations of ion-sensitive fluorophores by FCS offers selective advantages over other techniques for measuring local ion concentrations, and, in particular, for studying exchange kinetics of ions on a very local scale. This opens for several areas of application. The FCS approach was used to investigate fundamental aspects of proton exchange at and along biological membranes. The protonation relaxation rate, as measured by FCS for a pH-sensitive dye, can also provide information about local accessibility/interaction of a particular labeling site and conformational states of biomolecules, in a similar fashion as in a fluorescence quenching experiment. The same FCS concept can also be applied to ion exchange studies using other ion-sensitive fluorophores, and by use of dyes sensitive to other ambient conditions the concept can be extended also beyond ion exchange studies.
Authors:
Jerker Widengren
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Methods in enzymology     Volume:  519     ISSN:  1557-7988     ISO Abbreviation:  Meth. Enzymol.     Publication Date:  2013  
Date Detail:
Created Date:  2013-01-02     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0212271     Medline TA:  Methods Enzymol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  231-52     Citation Subset:  IM    
Copyright Information:
Copyright © 2013 Elsevier Inc. All rights reserved.
Affiliation:
Experimental Biomolecular Physics, Department of Applied Physics, Royal Institute of Technology (KTH), Albanova University Center, Stockholm, Sweden. Electronic address: jwideng@kth.se.
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