Protein-Protein Interactions Studied by NMR——A Review Using the Ubiquitin-Proteasome

Abstract

Abstract:

Protein-protein interactions (PPIs) play key roles in multiple cellular processes. Both X-ray crystallography and NMR techniques are commonly used to illustrate the structural basis of PPIs. Although most of the available structures of protein complexes are determined by X-ray crystallography, NMR proves to be the technique of choice under special circumstances such as crystallization-resistance, weak binding, and complicated dynamic behavior presented by protein complexes. Chemical shift perturbation analysis, inter-molecular NOE detection, paramagnetic relaxation enhancement and residual dipolar coupling detection are the four major NMR techniques used for studing PPI. The principles and strengths of these NMR techniques and their applications in studying the ubiquitin-proteasome pathway are reviewed in this article.

Key words: NMR, chemical shift perturbation, nuclear Overhauser effect, paramagnetic relaxation enhancement, residual dipolar coupling, ubiquitinproteasome pathway

CLC Number:

O482.53

ZHANG Nai-Xia, WU Juan, ZHANG Hua-Qun, LIU Xia. Protein-Protein Interactions Studied by NMR——A Review Using the Ubiquitin-Proteasome[J]. Chinese Journal of Magnetic Resonance, 2012, 29(2): 182-189.

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