Hydrogen exchange of the tryptophan residues in bovine ?-lactalbumin studied by uv spectroscopy
Author:
Publisher
Wiley
Subject
Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics
Reference39 articles.
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Cited by 10 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Transition state in the folding of α-lactalbumin probed by the 6-120 disulfide bond;Protein Science;1998-07
2. Conformational comparison between α-lactalbumin and lysozyme;Advances in Biophysics;1994
3. Conformational aspects of the Cu2+ binding to α-lactalbumin. Characterization and stability of the Cu-bound state;Biophysical Chemistry;1992-04
4. Effect of metal ions on the unfolding kinetics of α-lactalbumin on weakly hydrophobic surfaces;Journal of Chromatography A;1991-01
5. Intrinsic fluorescence studies of the kinetic mechanism of unfolding of α-lactalbumin on weakly hydrophobic chromatographic surfaces;Journal of Chromatography A;1990-02
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