Abstract
Human Fibroblast growth factor 1 (hFGF1) is a powerful signaling molecule belongs to FGF1 subfamily and a key member of biological process related to cell development and wound healing. Studies have revealed that under physiological temperatures, hFGF1 has low thermodynamic stability and biological activity. The Cysteine residues present in hFGF1 have a prominent effect on folding equilibrium of the protein. Studies to determine the contribution of these invariant cysteine residues to the inherent stability of the hFGF1 can lead to potential therapeutic application in the field of wound healing. Interestingly, mutational substitution of Cystein117 residue with alanine in hFGF1 has proven to govern the inherent stability and biological activity results. Detailed analysis of the results will be presented.
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