Folding and homodimerization of wheat germ agglutinin.

ABSTRACT: Wheat germ agglutinin (WGA) is emblematic of proteins that specialize in the recognition of carbohydrates. It was the first lectin reported to have a capacity for discriminating between normal and malignant cells. Since then, it has become a preferred model for basic research and is frequently considered in the development of biomedical and biotechnological applications. However, the molecular basis for the structural stability of this homodimeric lectin remains largely unknown, a situation that limits the rational manipulation and modification of its function. In this work we performed a thermodynamic characterization of WGA folding and self-association processes as a function of pH and temperature by using differential scanning and isothermal dilution calorimetry. WGA is monomeric at pH

SUBMITTER: Portillo-Tellez Mdel C 

PROVIDER: S-EPMC3177061 | biostudies-literature | 2011 Sep

REPOSITORIES: biostudies-literature