Abstract
Fibroblast Growth Factor-1 is a 16 kiloDalton heparin-binding protein whose function involves signaling cells for responses such as cell growth, differentiation, endurance, and response to trauma. FGF-1 also has restorative effects like wound healing, angiogenesis, and nerve repair. Wild type FGF-1 has a short half-life in vivo, and denatures at physiological temperature. Due to its instability and potential for therapeutics, a more stable form of FGF-1 is desirable.The purpose of the research study is to characterize the FGF-1 mutant, K126D using a series of techniques like CD, Fluorescence Spectroscopy, Differential Scanning Calorimetry, thermal denaturation, NMR spectroscopy, trypsin digestion, and ANS titration. These techniques will be used to assess the degree of stability of K126D as compared to wild type FGF-1. In addition, cell proliferation assays will be performed to determine how the mutation affects the activity of FGF-1.
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