Showing papers by "Yong-Bin Yan published in 2002"

Biphasic reductive unfolding of ribonuclease A is temperature dependent.

Abstract: The kinetics of the reversible thermal unfolding, irreversible thermal unfolding, and reductive unfolding processes of bovine pancreatic ribonuclease A (RNase A) were investigated in NaCl/Pi solutions Image parameters including Shannon entropy, Hamming distance, mutual information and correlation coefficient were used in the analysis of the CD and 1D NMR spectra The irreversible thermal unfolding transition of RNase A was not a cooperative process, pretransitional structure changes occur before the main thermal denaturation Different dithiothreitol (dithiothreitolred) concentration dependencies were observed between 303 and 313 K during denaturation induced by a small amount of reductive reagent The protein selectively follows a major unfolding kinetics pathway with the selectivity can be altered by temperature and reductive reagent concentration Two possible explanations of the selectivity mechanism were discussed

Two-state kinetics characterized by image analysis of nuclear magnetic resonance spectra

Abstract: Nuclear magnetic resonance (NMR) spectroscopy 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.