Helix-coil transition of poly- l-phenylalanine studied by nuclear magnetic resonance

Abstract

This chapter discusses the application of nuclear magnetic resonance (NMR) to protein chemistry primarily in terms of the information that the technique can contribute to the protein structure and function. The chapter examines information about proteins that can be derived from NMR spectra, the premises and procedures necessary to interpret the observations. It also discusses whether NMR is merely another method for confirming conclusions reached by other methods or does it, in fact, permit findings not obtainable otherwise. With the success of selective deuteration of proteins, the two major problems of protein NMR spectroscopy—resolution and assignment of resonance lines—have been shown to be soluble at least in principle. It is to be expected that future difficulties in overcoming these problems will be proportional to the complexity of the protein. Success, however, is to be sought in experimental ingenuity rather than through further advances in instrumentation.