J Physiol Volume 563, Number 1, 61-71, February 15, 2005 DOI: 10.1113/jphysiol.2004.081117
Quantitative functional analysis of protein complexes on surfaces
Hye Jin Lee3,
Yuling Yan2,
Gerard Marriott1 and
Robert M Corn3
1 Department of Physiology, University of Wisconsin–Madison, WI, USA
2 Department of Mechanical Engineering, University of Hawai'i Manoa, HI, USA
3 Department of Chemistry, University of California–Irvine, CA, USA
A major challenge in cell and molecular physiology research is to understand the mechanisms of biological processes in terms of the interactions, activities and regulation of the underlying proteins. Functional and mechanistic analyses of the large number of proteins that participate in the regulation of cellular processes will require new approaches and techniques for high throughput and multiplexed functional analyses of protein interactions, protein conformational dynamics and protein activity. In this review we focus on the development and application of proteomics and associated technologies for quantitative functional analysis of proteins and their complexes that include: (1) the application of surface plasmon resonance (SPR) imaging for multiplexed, label-free analyses of protein interactions, binding constants for biomolecular interactions and protein activities; and (2) high content analysis of protein motions within functional multiprotein complexes.
(Received 13 December 2004;
accepted after revision 16 December 2004;
first published online 21 December 2004)
Corresponding author G. Marriott: Department of Physiology, University of Wisconsin, 1300 University Ave., Madison, WI 53706, USA. Email: gm{at}physiology.wisc.edu
Copyright © 2005 The Physiological Society.
