Journal of Structural and Functional Genomics

, Volume 8, Issue 2, pp 67–72

Structural basis of protein–protein interaction studied by NMR

Original Paper

DOI: 10.1007/s10969-007-9021-8

Cite this article as:
Shi, Y. & Wu, J. J Struct Funct Genomics (2007) 8: 67. doi:10.1007/s10969-007-9021-8

Abstract

This paper describes efforts of the structural genomics project in the nuclear magnetic resonance (NMR) laboratory at the University of Science and Technology of China. This structural genomics project is biological-functional driven. Targets are mainly selected from two systems: proteins related with regulation of gene expression in humans and other eukaryotes, and proteins existing in the cell junction in humans. The majority of proteins selected from these two systems are related with human health and diseases, and some are potential drug targets. Twenty-five protein structures from Homo sapiens and other eukaryotes have been determined during last 5 years in this laboratory. Nuclear magnetic resonance (NMR) spectroscopy is highly suited to investigate molecular interactions at a close physiological condition and is particularly suited for the study of low-affinity, transient complexes. It can provide information on protein surface interaction, their complex structure, and their dynamic properties during protein recognition. Several examples are given in this paper.

Keywords

NMR spectroscopy Protein–protein interaction Protein structure Sample preparation Structural genomics Target selection 

Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  1. 1.Hefei National Laboratory for Physical Sciences at Microscale and School of Life SciencesUniversity of Science and Technology of ChinaHefeiPeople’s Republic of China

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