ISSN: 2641-9165
Authors: Nasreen K, Md. Ali Imam and Islam A*
The folding of protein into their compact three dimensional structures has enabled living organisms to develop astonishing diversity and selectivity in their underlying chemical processes generating biological activity, the trafficking of molecules to specific cellular locations and the regulation of cellular growth and differentiation. All these processes require long term stability of proteins and only correctly folded proteins possess this attribute. This study has investigated the effect of glucose on thermal stability of myoglobin. We monitored the heme protein interaction at 409 nm and polypeptide backbone at 222 nm. It seems that the glucose molecule is stabilizing protein heme interaction while destabilising overall peptide backbone.
Keywords: Myoglobin; Osmolytes; Spectroscopy; Circular dichroism; Molecular docking
