Abstract
Using fluorescence correlation spectroscopy, we measured a dissociation constant of 20 nM between EGFP-labeled LcrV from Yersinia pestis and its cognate membrane-bound protein YopB inserted into a lipid nanodisc. The combination of fluorescence correlation spectroscopy and nanodisc technologies provides a powerful approach to accurately measure binding constants of interactions between membrane bound and soluble proteins in solution. Straightforward sample preparation, acquisition, and analysis procedures make this combined technology attractive for accurately measuring binding kinetics for this important class of protein-protein interactions.
| Original language | English (US) |
|---|---|
| Journal | Biophysical Journal |
| Volume | 106 |
| Issue number | 2 |
| DOIs | |
| State | Published - Jan 21 2014 |
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ASJC Scopus subject areas
- Biophysics
Cite this
Quantifying interactions of a membrane protein embedded in a lipid nanodisc using fluorescence correlation spectroscopy. / Ly, Sonny; Bourguet, Feliza; Fischer, Nicholas O; Lau, Edmond Y; Coleman, Matthew A; Laurence, Ted A.
In: Biophysical Journal, Vol. 106, No. 2, 21.01.2014.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Quantifying interactions of a membrane protein embedded in a lipid nanodisc using fluorescence correlation spectroscopy
AU - Ly, Sonny
AU - Bourguet, Feliza
AU - Fischer, Nicholas O
AU - Lau, Edmond Y
AU - Coleman, Matthew A
AU - Laurence, Ted A.
PY - 2014/1/21
Y1 - 2014/1/21
N2 - Using fluorescence correlation spectroscopy, we measured a dissociation constant of 20 nM between EGFP-labeled LcrV from Yersinia pestis and its cognate membrane-bound protein YopB inserted into a lipid nanodisc. The combination of fluorescence correlation spectroscopy and nanodisc technologies provides a powerful approach to accurately measure binding constants of interactions between membrane bound and soluble proteins in solution. Straightforward sample preparation, acquisition, and analysis procedures make this combined technology attractive for accurately measuring binding kinetics for this important class of protein-protein interactions.
AB - Using fluorescence correlation spectroscopy, we measured a dissociation constant of 20 nM between EGFP-labeled LcrV from Yersinia pestis and its cognate membrane-bound protein YopB inserted into a lipid nanodisc. The combination of fluorescence correlation spectroscopy and nanodisc technologies provides a powerful approach to accurately measure binding constants of interactions between membrane bound and soluble proteins in solution. Straightforward sample preparation, acquisition, and analysis procedures make this combined technology attractive for accurately measuring binding kinetics for this important class of protein-protein interactions.
UR - http://www.scopus.com/inward/record.url?scp=84892734192&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=84892734192&partnerID=8YFLogxK
U2 - 10.1016/j.bpj.2013.12.014
DO - 10.1016/j.bpj.2013.12.014
M3 - Article
C2 - 24461026
AN - SCOPUS:84892734192
VL - 106
JO - Biophysical Journal
JF - Biophysical Journal
SN - 0006-3495
IS - 2
ER -