Unfolding Studies of the Cysteine Protease Baupain, a Papain-Like Enzyme from Leaves of Bauhinia forficata: Effect of pH, Guanidine Hydrochloride and Temperature

Unfolding Studies of the Cysteine Protease Baupain, a Papain-Like Enzyme from Leaves of Bauhinia forficata: Effect of pH, Guanidine Hydrochloride and Temperature

Baupain belongs to the α+β class of proteins with a secondary structure-content of 44% α-helix, 16% β-sheet and 12% β-turn. The structural transition induced by pH was found to be noncooperative, with no important differences observed in the pH range from 3.0 to 10.5. At pH 2.0 the protein presente...

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Bibliographic Details
Main Authors: Rosemeire A. Silva-Lucca, Sheila S. Andrade, Rodrigo Silva Ferreira, Misako U. Sampaio, Maria Luiza V. Oliva
Format: Article
Language:English
Published: MDPI AG 2013-12-01
Series:Molecules
Subjects:
baupain
circular dichroism
cysteine protease
papain
protein conformation
Online Access:http://www.mdpi.com/1420-3049/19/1/233

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