Date of Graduation


Document Type


Degree Name

Bachelor of Science

Degree Level



Chemistry & Biochemistry


Kumar, T.K.S.

Committee Member/Reader

Ivey, Mack

Committee Member/Second Reader

Kumar, T.K.S.

Committee Member/Third Reader

Evans, Timothy

Committee Member/Fourth Reader

Caldwell, Stephen


Human acidic fibroblast growth factor 1 (FGF-1) is a potent modulator of cell survival and exhibits a universal role in various physiological processes. Though potent, FGF-1 unbound to heparin is known to show a poor thermal stability and a relatively short in vivo half-life. Much is known about the structure and relation of FGF-1 with heparin yet there is still unknown information regarding the exact role of heparin in stabilizing FGF-1. Thus, the aim of this study is to mutate glycine at position 134 to glutamic acid in wild type FGF1. G134 is located in the heparin binding pocket, thus the effects of this mutant will provide direct information on the interaction between heparin and the mutant form of FGF1. Because G134 is in close proximity to residues R136 and R133, the incorporation of glutamic acid, a negatively charged residue, in the heparin binding pocket might contribute to the formation of new electrostatic interactions in the binding pocket that would plausibly affect the binding affinity of FGF1 to heparin. FGF-1 G134E has been characterized using various biophysical methods. Results of the mutant characterization will be discussed in greater detail.