Dumoulin Mireille, Kumita Janet R, Dobson Christopher M
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK.
Acc Chem Res. 2006 Sep;39(9):603-10. doi: 10.1021/ar050070g.
Studies of lysozyme have played a major role over several decades in defining the general principles underlying protein structure, folding, and stability. Following the discovery some 10 years ago that two mutational variants of lysozyme are associated with systemic amyloidosis, these studies have been extended to investigate the mechanism of amyloid fibril formation. This Account describes our present knowledge of lysozyme folding and misfolding, and how the latter can give rise to amyloid disease. It also discusses the significance of these studies for our general understanding of normal and aberrant protein folding in the context of human health and disease.
几十年来，溶菌酶研究在确定蛋白质结构、折叠和稳定性的一般原理方面发挥了重要作用。大约10年前发现溶菌酶的两种突变变体与系统性淀粉样变性有关，之后这些研究扩展到对淀粉样纤维形成机制的研究。本综述介绍了我们目前对溶菌酶折叠和错误折叠的认识，以及后者如何导致淀粉样疾病。它还讨论了这些研究对于我们在人类健康和疾病背景下对正常和异常蛋白质折叠的总体理解的意义。
