Document Detail


Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions.
MedLine Citation:
PMID:  23533209     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
Surface plasmon resonance (SPR) is a powerful technique for monitoring the affinity and selectivity of biomolecular interactions. SPR allows for analysis of association and dissociation rate constants and modeling of biomolecular interaction kinetics, as well as for equilibrium binding analysis and ligand specificity studies. SPR has received much use and improved precision in classifying protein-protein interactions, as well as in studying small-molecule ligand binding to receptors; however, lipid-protein interactions have been underserved in this regard. With the field of lipids perhaps the next frontier in cellular research, SPR is a highly advantageous technique for cell biologists, as newly identified proteins that associate with cellular membranes can be screened rapidly and robustly for lipid specificity and membrane affinity. This technical perspective discusses the conditions needed to achieve success with lipid-protein interactions and highlights the unique lipid-protein interaction mechanisms that have been elucidated using SPR. It is intended to provide the reader a framework for quantitative and confident conclusions from SPR analysis of lipid-protein interactions.
Authors:
Robert V Stahelin
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Molecular biology of the cell     Volume:  24     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-03-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  883-6     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, Indiana University School of Medicine-South Bend, South Bend, IN 46617; Department of Chemistry and Biochemistry, University of Notre Dame, Notre Dame, IN 46556.
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