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Single disulfide bond reduced papain exists in a compact intermediate state
1Molecular Biology Unit, Institute of Medical Sciences, Banaras Hindu University, 221 005, Varanasi, India.
Biochimica Et Biophysica Acta
|June 23, 2000
Summary
Partially reducing papain exposes hydrophobic regions and expands its structure, altering its unfolding behavior. This modified protein derivative shows decreased stability and non-cooperative unfolding compared to the intact molecule.
Area of Science:
- Biochemistry
- Protein Chemistry
- Structural Biology
Background:
- Chemically modified proteins serve as models for studying protein folding in vivo.
- Protein reduction leads to conformational changes, affecting compactness and structure.
Purpose of the Study:
- To investigate the structural and unfolding properties of partially reduced papain.
- To characterize the derivative '3RCM papain' obtained by partial reduction in 8 M urea.
Main Methods:
- Spectroscopic methods (e.g., fluorescence quenching)
- Hydrodynamic studies
- Chemical denaturation (Guanidine hydrochloride)
- Thermal unfolding
Main Results:
- 3RCM papain retains significant secondary and tertiary structure but exhibits exposed hydrophobic regions and an expanded conformation.
- Unfolding studies revealed non-cooperative transitions and reduced thermal stability compared to intact papain.
- Partial reduction significantly impacts papain's overall unfolding behavior.
Conclusions:
- Partial reduction of papain leads to significant conformational changes and altered unfolding characteristics.
- The modified papain derivative (3RCM papain) serves as a valuable model for understanding protein structural dynamics.