The Denatured States of Lysozyme

1973 ◽  
Vol 51 (5) ◽  
pp. 581-585 ◽  
Author(s):  
M. Kugimiya ◽  
C. C. Bigelow

The denaturation of hen egg-white lysozyme has been studied under a variety of denaturing conditions by difference spectroscopy, polarimetry, and viscometry. It has been found that the lysozyme molecule can take up four different denatured conformations, depending on the denaturant used. Urea and guanidinium chloride produce the most completely denatured state, IV, and, listed in the order of increasing residual structure, lithium chloride gives state III, temperature state II, and lithium perchlorate state I. Differences in the spectra at 300 nm have been a valuable aid in relating the different denatured states to each other.

2014 ◽  
Vol 2014 ◽  
pp. 1-5 ◽  
Author(s):  
Gang Ma ◽  
Hong Zhang ◽  
Jianhua Guo ◽  
Xiaodan Zeng ◽  
Xiaoqian Hu ◽  
...  

The inhibitory effect of rifampicin on the amyloid formation of hen egg white lysozyme was assessed with both Thioflavin T (ThT) fluorescence assay and Fourier transform infrared (FTIR) difference spectroscopy. We reveal that ThT fluorescence assay gives a false positive result due to rifampicin interference, while FTIR difference spectroscopy provides a reliable assessment. With FTIR, we show that rifampicin only has marginally inhibitory effect. We then propose that FTIR difference spectroscopy can potentially be a convenient method for inhibitor screening in amyloid study.


1992 ◽  
Vol 14 (2) ◽  
pp. 237-248 ◽  
Author(s):  
Sheena E. Radford ◽  
Matthias Buck ◽  
Karen D. Topping ◽  
Christopher M. Dobson ◽  
Philip A. Evans

1997 ◽  
Vol 94 ◽  
pp. 356-364 ◽  
Author(s):  
M Faraggi ◽  
E Bettelheim ◽  
M Weinstein

2021 ◽  
pp. 138830
Author(s):  
Baoliang Ma ◽  
Haohao Wang ◽  
Yujie Liu ◽  
Fang Wu ◽  
Xudong Zhu

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