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Surface Plasmon Resonance - Mass Spectrometry

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Air date: Tuesday, November 12, 2002, 2:00:00 PM
Time displayed is Eastern Time, Washington DC Local
Views: Total views: 31 * This only includes stats from October 2011 and forward.
Category: Special
Runtime: 00:42:16
Description: The characterization of protein interactions: protein-protein, protein-DNA or protein-ligand, is central to the elucidation of the role of proteins in vivo. A key technique for studying these interactions is surface plasmon resonance (SPR) spectroscopy. Using SPR, kinetic studies can be performed on the binding of analytes to targets bound to a chip surface. While SPR is exquisitely sensitive, the detection of binding partners is non-specific. To address this concern, and to take advantage of the inherent affinity capture abilities of the SPR chips used, several groups have focused on combining SPR with mass spectrometry. The purpose of this discussion will be an introduction to the principles of SPR and recent advances in interfacing SPR with mass spectrometry. In addition, our recent work combining MALDI with SPR for the characterization of HIV nucleocapsid protein (NCp7) will be presented.

Mass Spectrometry Interest Group
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NLM Title: Surface plasmon resonance--mass spectrometry [electronic resource] / Jack Simpson.
Author: Simpson, Jack.
National Institutes of Health (U.S.)
Subjects: Mass Spectrometry
Surface Plasmon Resonance
Viral Proteins--analysis
Publication Types: Lectures
Rights: This is a work of the United States Government. No copyright exists on this material. It may be disseminated freely.
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NLM Classification: QC 454.M3
NLM ID: 101267834
CIT Live ID: 2001
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