Abstract
The aim of protein folding studies is to understand the relationship between the information encoded in the linear amino acid sequence of a polypeptide chain and its three-dimensional structure. The elucidation of the kinetic folding mechanism of a protein is the first step on the way to characterize its complete folding pathway. Subsequent steps comprise the characterization of transiently formed intermediates and of the transition states between the various states of the protein. A folding pathway is understood when all transient intermediates and the transition states between them are characterized. This chapter deals with several aspects of the process of determining folding pathways. The elucidation of kinetic folding mechanisms under various solvent conditions will be described and methods used in the characterization of the transition states for individual folding reactions will be discussed. The detailed characterization of folding intermediates is described in Chapters 13 and Chapter 15.
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