Protein folding and stability: the pathway of folding of barnase

FEBS Letters

Fersht, Alan R.¹ 

[1] Cambridge Centre for Protein Engineering, MRC Centre and Department of Chemistry, Cambridge, UK

关键词: Protein engineering;    Protein folding;    Protein stability;    Bamase;   

DOI  :  10.1016/0014-5793(93)81405-O

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The pathway of folding of a protein will be completely solved when the structures and energetics of the initial unfolded states, all folding intermediates, all transition states and the final folded state, have been determined. The ultimate goal is to analyse, at the detail of individual residues, the non-covalent interactions that are primarily responsible for dictating secondary and tertiary structure. Until recently, the tools for tackling such a daunting task were quite inadequate, but recent developments in NMR and protein engineering have made it possible to determine crucial features in the folding process. It now seems feasible that sufficient experimental detail will be obtained to provide general principles that govern protein folding and provide the basis for its rigorous theoretical analysis. This lecture will outline the progress and prospects in attainment of the goals as applied to the small ribonuclease, barnase.

【 授权许可】

Unknown