| 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 |
Related Documents
:
|
7671633 - Structural characterization of clear human lens lipid membranes by near-infrared fourie... 23447533 - Polar residues and their positional context dictate the transmembrane domain interactio... 7612833 - Structure and phase behavior of lipid suspensions containing phospholipids with covalen... |
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. |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Interactions in gene expression networks studied by two-photon fluorescence fluctuation spectroscopy...
Next Document: Fluctuation analysis of activity biosensor images for the study of information flow in signaling pat...