Understanding how proteins fold: the lysozyme story so far

doi:10.1016/0968-0004(94)90171-6

Trends in Biochemical Sciences

Volume 19, Issue 1, January 1994, Pages 31-37

https://doi.org/10.1016/0968-0004(94)90171-6 Get rights and content

Abstract

Hen lysozyme is one of the best characterized and most studied of all proteins. Recently, we have used a range of different methods to examine the events involved in the in vitro folding pathway of this protein. In this review we show that, by combining complementary techniques, it has been possible to piece together a detailed model for the folding of this enzyme. Important questions prompted by this work are highlighted and we then propose some ideas consistent with our data, as well as those of others, which we believe begin to provide insight into one of the most intriguing of structural problems in biology - how proteins can achieve their complex native forms from disordered denatured states.

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Trends in Biochemical Sciences

ReviewUnderstanding how proteins fold: the lysozyme story so far

Abstract

Curr. Opin. Struct. Biol.

J. Mol. Biol.

Curr. Opin. Struct. Biol.

J. Mol. Biol.

J. Chim. Phys.

Protein Science

Annu. Rev. Biochem.

Nature

Nature

Science

Prot. Struct. Funct. Genet.

Prot. Struct. Funct. Genet.

Biochemistry

Biochemistry

Biochemistry

Science

Prot. Struct. Funct. Genet.

Review
Understanding how proteins fold: the lysozyme story so far