[RASMB] Use of SDS to study peptide

[John E Harlan]

Karen-

Did your non-ideality occur only in sedimentation equilibrium experiments, 
or did you see problems in sed. velocity as well. 

John




Karen Fleming <Karen.Fleming at jhu.edu>
Sent by: rasmb-bounces at server1.bbri.org
01/12/2006 11:29 AM

 
        To:     Damien Thévenin <damien at UDel.Edu>
        cc:     rasmb at server1.bbri.org, (bcc: John E Harlan/LAKE/PPRD/ABBOTT)
        Subject:        Re: [RASMB] Use of SDS to study peptide


I tried it a couple of times with glycophorin and the high charge 
density of the micelles caused a lot of nonideality in the 
sedimentation profiles. We could never fit the data and so abandoned 
SDS for other detergents. The charge density also causes nonideality in 
fluorescence experiments.
-Karen Fleming
On Jan 12, 2006, at 11:04 AM, Damien Thévenin wrote:

> Hello all,
>
> I study transmembrane (TM) peptides interaction in various detergents 
> (DPC, C8E5, C14-betaine,...) and I would like to know whether SDS is 
> an suitable detergent for AUC. Indeed, I haven't seen any paper 
> reporting the use of SDS to study TM peptides by AUC. Furthermore, SDS 
> is my detergent of choice when I study these same peptides by CD or 
> fluorescence. So, does SDS have properties that make it unsuitable for 
> AUC?
> Thanks for your help and insights.
>
> Damien
>
> ----------
> Damien Thévenin
>
> Department of Chemistry & Biochemistry
> University of Delaware
> Delaware Biotechnology Institute
> 15 Innovation way (room 146)
> Newark, DE 19711
>
> Phone     302.831.4410
> FAX         302.831.3447
> damien at udel.edu
>
>
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Karen G. Fleming, Ph.D.
Assistant Professor
Thomas C. Jenkins Department of Biophysics
Johns Hopkins University
3400 North Charles Street
Baltimore, MD 21218

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