27] Structure and thermal stability of phage T4 lysozyme

Abstract

Publisher Summary This chapter discusses the phage T4 lysozyme system. Methods of rapidly generating mutants, characterizing their thermal stability, and accurately determining their X-ray crystal structures are discussed. Results and insights into the structural basis of protein thermal stability are summarized. Phage T4 lysozyme provides a powerful model system for studying the structural basis of protein thermal stability. By comparing the properties of mutant and wild-type proteins, the contributions of individual chemical groups can be estimated. The diversity of substitutions in the collection of mutant lysozymes indicates that many types of interactions contribute to stability. Despite great advances in the technology of generating and studying mutants, the fundamental problem of assigning the observed effects to the energy of the folded or unfolded state remains unsolved. One approach to overcome this limitation is to look for structural patterns in the native conformation that are associated with thermal stability.