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Pea Lectin in Alkaline Conditions: Formation of Molten Globule-Like Intermediate and Its Structural and Thermal Studies Under the Influence of Hexafluoroisopropanol

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Pea lectin was exposed to a pH range of 7-13. It was observed that alkaline-unfolding resulted in a molten globule-like intermediate at pH 11. The structural stability of this alkaline unfolded molten globule-like state of pea lectin was studied in the presence of HFIP. Thermal studies showed that this state was more susceptible to thermal denaturation as compared to the native state and it became even more so in presence of HFIP.

Keywords: Alkaline unfolding; HFIP induced state; MG-like state; pea lectin

Document Type: Research Article


Publication date: 2008-07-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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