這篇研究在描述酸性人類纖維母細胞生長因子(h-FGF)的開散及折疊路徑之性質。第一章提供一些非數字但有深度的介紹有關這一方面的研究報導。第二章是有關h-FGF的表現、純化及性質的報導。在第三章會提供hFGF的平衡中間物（equilibrium intermediate)之定義及性質的詳細探討。我們發現在Gdn-HCl濃度接近1M時，h-FGF有一似融狀小球的中間物存在。當使用一些生物物理技術如多維NMR去研究這個中間物時，發現它和活性態（active state)的h-FGF有相似的結構性質。在第四章將討論h-FGF的再折疊動力學（refolding kinetics)；我們觀察到h-FGF可以由在尿素的開散態緩慢地再折疊回去（>50sec)。當蛋白質在再折疊的過程中並沒有產生疏水性的瓦解或產生一個穩定的動力學中間物。當我們使用quench-flow NMR進行監測時，我們首度發現在h-FGF的再折疊路徑中N端及C端互相作用產生氫鍵。最後，在第五章我們將探討osmolytes扮演的角色，以proline為例，在再折疊過程中它可以防止蛋白質凝聚；proline的似保護的活性可歸因於形成一個超分子組合（supramolecular assembly)。可以想像地，這個超分子組合提供必要的疏水性接觸給再折疊蛋白質的溶劑暴露及非極性表面，使其避免掉凝聚的產生。這篇研究提供了一些有關蛋白質折疊及開散的新資訊，以期能提供一些新的設計於未來的研究。

The present study describes the characterization of the unfolding and refolding pathways of the acidic human fibroblast growth factor (hFGF-1). The first chapter provides an updated, concise but in-depth introduction to the various topics which are relevant to the research elaborated in this study. The second chapter of the thesis reports the expression, purification and characterization of hFGF-1. A detailed account of the identification and characterization of an equilibrium intermediate is provided in Chapter-III of the thesis. It is found that hFGF-1 exists in a molten-globule-like intermediate at a guandinie hydrochloride concentration close to 1M. Using a variety of biophysical techniques including multidimensional NMR, the equilibrium intermediate is shown to have structural character(s) resembling that of the native state. The refolding kinetics of hFGF-1 is discussed in detail in Chapter-IV of the thesis. It is observed that hFGF-1 refolds from its urea unfolded state very slowly (> 50 seconds) but yet co-operatively. The refolding of the protein proceeds without hydrophobic collapse or formation of stable kinetic intermediates. The chronology of refolding events monitored by quenched-flow NMR revealed that hydrogen bond formation between the N- and C- terminal ends is the first detectable event in the refolding pathway of hFGF-1. Finally, in Chapter V, the role of osmolytes, such as proline in the prevention of aggregation during protein refolding is investigated. It is observed that proline effectively thwarts protein aggregation and helps the protein to regain its native state. The chaperone-like activity of proline is attributed to its ability to form a supramolecular assembly. It is envisaged that the supramolecular assemblies of proline provides the necessary hydrophobic contacts to the solvent exposed, non-polar surface(s) of the refolding protein and consequently prevents aggregation The research described herein offers several new leads which could be successfully exploited to formulate important and interesting research projects in the future.

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