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Detecting Native Protein Interaction
and Phosphorylation:
New Approaches and Novel Technologies

Event Date: Wednesday, November 9, 2011 12:00 noon ET; 9 a.m. PT; 5 p.m. GMT, 6 p.m. CEST

Few, if any, proteins carry out their function in isolation. More likely is that they interact with one or more other proteins, during which conformational changes and even physical modifications such as phosphorylation may occur. The ability to detect both the interaction and modification of proteins is critical to elucidating function and dysfunction in cells and tissues, leading to a deeper understanding of normal as well as diseased states. This webinar will focus on current methodologies available to study protein-protein interactions, as well as looking at new technologies for characterizing protein binding events in a noninvasive manner that more closely resembles a cell's natural environment, producing more physiologically relevant data.

During the webinar, our expert panelists will:

Explain how protein structure and function can be affected by posttranslational modifications and interactions with diverse partners
Discuss current state-of-the-art methods and technologies for characterizing protein-protein interactions and modifications
Describe how multiplexing can be used to distinguish similar biomolecular events, such as multiphosphorylated molecules or multiple interacting partners
Answer your questions live and in real time!

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1. What are the main limitations you face when detecting protein-protein interactions? Check all that apply

Sensitivity

Throughput

Flexibility

Instrumentation

Cross-validation

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2. What techniques do you use to detect protein-protein interactions? Check all that apply

Pull-down/Co-immunoprecipitation

FRET/BRET

Mass spectrometry

AlphaScreen

SPR (Biacore)

Isothermal calorimetry

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3. If you currently use biochemical assays, would you like to move to cell-based assays? Select one

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