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Positron annihilation studies in lysozyme and catalase
Y Rohilla1, K P Singh, S R Choudhury
1Department of Physics, G.B. Pant University of Agriculture & Technology, Pantnagar, India.
Indian Journal of Biochemistry & Biophysics
|December 1, 1992
Summary
Positron annihilation spectroscopy reveals temperature-dependent changes in enzyme structures like lysozyme and catalase. These findings, explained by the free volume model, offer new insights into enzyme bioactivity mechanisms.
Area of Science:
- Biophysics
- Enzymology
- Materials Science
Background:
- Enzyme structure and dynamics are crucial for biological activity.
- Understanding enzyme conformational changes can elucidate bioactivity mechanisms.
Purpose of the Study:
- Investigate the temperature dependence of positron lifetimes in lysozyme and catalase.
- Provide new insights into enzyme bioactivity using positron annihilation studies.
Main Methods:
- Positron annihilation spectroscopy was employed.
- Measurements were conducted on lysozyme and catalase across a temperature range.
Main Results:
- Positron lifetimes exhibited temperature dependence in both enzymes.
- Observed changes are consistent with the free volume model.
Conclusions:
- Fluctuations in enzyme conformational microstates influence positron lifetimes.
- Positron annihilation studies offer a novel approach to understanding enzyme bioactivity.