Please use this identifier to cite or link to this item: https://doi.org/10.1021/jp911720w
DC FieldValue
dc.titleConcentration-dependent aggregation of CHAPS investigated by NMR spectroscopy
dc.contributor.authorQin, X.
dc.contributor.authorLiu, M.
dc.contributor.authorYang, D.
dc.contributor.authorZhang, X.
dc.date.accessioned2014-10-27T08:24:29Z
dc.date.available2014-10-27T08:24:29Z
dc.date.issued2010-03-25
dc.identifier.citationQin, X., Liu, M., Yang, D., Zhang, X. (2010-03-25). Concentration-dependent aggregation of CHAPS investigated by NMR spectroscopy. Journal of Physical Chemistry B 114 (11) : 3863-3868. ScholarBank@NUS Repository. https://doi.org/10.1021/jp911720w
dc.identifier.issn15206106
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100318
dc.description.abstractCHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate) is a zwitterionic surfactant, which has been extensively used in various biological fields. In the present work, the concentration-dependent aggregation of the surfactant in deuterium oxide solution was investigated by NMR spectroscopy. We have found that two break points exist on the basis of the NMR parameters such as chemical shift difference (Δδ), self-diffusion coefficient (D), and relaxation rates (R1 R2). The first break point corresponds to the widely accepted normal critical micelle concentration (cmc). The second one is unexpected and ascribed to the second cmc, indicating that there is another type of micelle at higher concentrations. Further analysis using ID selective NOESY with spin-diffusion quenching reveals that at the concentration above the second cmc CHAPS may form a two-layer spherical structure of micelles, with the aliphatic groups of CHAPS molecules in the inner layer interact with the steroid groups in the outer layer. The existence of two types of micelles has also been supported by our TEM experiment. The dependence of CHAPS micelle size on concentration explains why some proteins are soluble and stable only at concentrations above the second cmc. Therefore, our finding provides a basis for optimizing CHAPS concentration in functional and structural studies of membrane proteins. © 2010 American Chemical Society.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1021/jp911720w
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1021/jp911720w
dc.description.sourcetitleJournal of Physical Chemistry B
dc.description.volume114
dc.description.issue11
dc.description.page3863-3868
dc.description.codenJPCBF
dc.identifier.isiut000275710400017
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

23
checked on Jul 17, 2019

WEB OF SCIENCETM
Citations

23
checked on Jul 17, 2019

Page view(s)

43
checked on May 25, 2019

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.