NMR Studies of Amino Acids, Peptides, and Proteins: A Brief Review, 1980-1982

Publisher Summary This chapter reviews the development studies in the field of Nuclear Magnetic Resonance (NMR) of amino acids, peptides, and proteins for the three-year period from 1980 to 1982. These three years were marked by a steady advance in NMR methods. The improvements were principally in magnets and in the computation facility dedicated to each machine. The large core memories and fully interactive use of disk storage have not only made instruments more efficient in the use of time but have also permitted the development of two-dimensional methods. The mainstream of amino acid studies concentrate on their use as simple systems for the testing of new techniques or theories. Cross-relaxation effects in the photochemically induced dynamic nuclear polarization (photo-CIDNP) spectra of N -acetyltyrosine and N -acetyltryptophan have been used in order to assess the possibilities for observing population transfer between amino acids in proteins. In proline-containing peptides, the 15 N nucleus is very sensitive to conformational changes induced by cis/trans isomerism of the proline. These effects are largely long range and depend on both the amino acid side chains and the solvent.