摘要
Nuclear magnetic resonance (NMR) spectros-copy has become an important tool in modern biological research. NMR spectra image analysis can be used to analyze the kinetics of biomacromolecular conformational changes. The relationship between the image parameters and the protein dynamics was investigated by using a small globular protein ω-conotoxin SO3 (ω-CTX SO3). The physical meanings of the image parameters were characterized from the results. Comparison of the data from the traditional integral area of specific resonance peaks method and the NMR image analysis method showed the advantages of using NMR spectra image analysis for kinetic analysis of two-state processes monitored by 1D proton NMR.
Nuclear magnetic resonance (NMR) spectros-copy has become an important tool in modern biological research. NMR spectra image analysis can be used to analyze the kinetics of biomacromolecular conformational changes. The relationship between the image parameters and the protein dynamics was investigated by using a small globular protein w-conotoxin SO3 (w-CTX SO3). The physical meanings of the image parameters were characterized from the results. Comparison of the data from the traditional integral area of specific resonance peaks method and the NMR image analysis method showed the advantages of using NMR spectra image analysis for kinetic analysis of two-state processes monitored by 1D proton NMR.
基金
This work was supported by the National Key Basic Research Special Funds of China (Grant No. G1999075607)
the 985 Funds of Tsinghua University
and the THSJZ of Tsinghua University, China.
