High-throughput analysis of GST-fusion protein expression and activity-dependent protein interactions on GST-fusion protein arrays with a spectral surface plasmon resonance biosensor

PROTEOMICS ◽  
2006 ◽  
Vol 6 (4) ◽  
pp. 1110-1120 ◽  
Author(s):  
Jae-Wan Jung ◽  
Se-Hui Jung ◽  
Hyun-Soo Kim ◽  
Jong Seol Yuk ◽  
Jae-Bong Park ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Fusion Protein ◽  
Protein Interactions ◽  
High Throughput Analysis ◽  
Protein Arrays ◽  
Fusion Protein Expression ◽  
Dependent Protein ◽  
Gst Fusion Protein ◽  
Activity Dependent ◽  
Expression And Activity

A fusion protein expression analysis using surface plasmon resonance imaging

2004 ◽  
Vol 330 (2) ◽  
pp. 251-256 ◽  
Author(s):  
Jin-Mi Jung ◽  
Yong-Beom Shin ◽  
Min-Gon Kim ◽  
Hyeon-Su Ro ◽  
Hee-Tae Jung ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Fusion Protein ◽  
Protein Expression ◽  
Surface Plasmon ◽  
Expression Analysis ◽  
Plasmon Resonance ◽  
Surface Plasmon Resonance Imaging ◽  
Resonance Imaging ◽  
Fusion Protein Expression

Analysis of protein interactions on protein arrays by a wavelength interrogation-based surface plasmon resonance biosensor

PROTEOMICS ◽  
2004 ◽  
Vol 4 (11) ◽  
pp. 3468-3476 ◽  
Author(s):  
Jong Seol Yuk ◽  
Se-Hui Jung ◽  
Jae-Wan Jung ◽  
Duk-Geun Hong ◽  
Jeong-A Han ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interactions ◽  
Plasmon Resonance ◽  
Protein Arrays ◽  
Surface Plasmon Resonance Biosensor

Analysis of protein interactions on protein arrays by a novel spectral surface plasmon resonance imaging

2006 ◽  
Vol 21 (8) ◽  
pp. 1521-1528 ◽  
Author(s):  
Jong Seol Yuk ◽  
Hyun-Soo Kim ◽  
Jae-Wan Jung ◽  
Se-Hui Jung ◽  
Seung-Joon Lee ◽  
...  
Keyword(s):  
Surface Plasmon Resonance ◽  
Surface Plasmon ◽  
Protein Interactions ◽  
Plasmon Resonance ◽  
Surface Plasmon Resonance Imaging ◽  
Resonance Imaging ◽  
Protein Arrays

scholarly journals Activity-dependent changes in synaptic protein complex composition are consistent in different detergents despite differential solubility

2019 ◽  
Author(s):  
Jonathan D. Lautz ◽  
Edward P. Gniffke ◽  
Emily A. Brown ◽  
Karen B. Immendorf ◽  
Ryan D. Mendel ◽  
...  
Keyword(s):  
Protein Interactions ◽  
Protein Complexes ◽  
Synaptic Activity ◽  
Synaptic Proteins ◽  
Size Exclusion ◽  
Synaptic Protein ◽  
Exclusion Chromatography ◽  
Associated Proteins ◽  
Dependent Protein ◽  
Activity Dependent

AbstractAt the post-synaptic density (PSD), large protein complexes dynamically form and dissociate in response to synaptic activity, comprising the biophysical basis for learning and memory. The use of detergents to both isolate the PSD fraction and release its membrane-associated proteins complicates studies of these activity-dependent protein interaction networks, because detergents can simultaneously disrupt the very interactions under study. Despite widespread recognition that different detergents yield different experimental results, the effect of detergent on activity-dependent synaptic protein complexes has not been rigorously examined. Here, we characterize the effect of three detergents commonly used to study synaptic proteins on activity-dependent protein interactions. We first demonstrate that SynGAP-containing interactions are more abundant in 1% Deoxycholate (DOC), while Shank-, Homer-and mGluR5-containing interactions are more abundant in 1% NP-40 or Triton. All interactions were detected preferentially in high molecular weight (HMW) complexes generated by size exclusion chromatography, although the detergent-specific abundance of proteins in HMW fractions did not correlate with the abundance of detected interactions. Activity-dependent changes in protein complexes were consistent across detergent types, suggesting that detergents do not isolate distinct protein pools with unique behaviors. However, detection of activity-dependent changes is more or less feasible in different detergents due to baseline solubility. Collectively, our results demonstrate that detergents affect the solubility of individual proteins, but activity-dependent changes in protein interactions, when detectable, are consistent across detergent types.

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