Use of chemical shifts and coupling constants in nuclear magnetic resonance structural studies on peptides and proteins.

摘要: Publisher Summary This chapter describes advances in the use of coupling constants and chemical shifts structural studies peptides proteins. Coupling constant information can be incorporated into input data for structure calculations, giving direct on dihedral angles stereospecific assignments prochiral groups such as β-methylene protons methyl leucine valine. Because complexity interactions that influence shift each nucleus, this type is more useful at refinement stage. However, determination protein peptide using from nuclear magnetic resonance (NMR) experiments solution now a well-established method, it frequently used an adjunct to X-ray crystal determination, well cases where crystals are unavailable. With increasing size proteins which three-dimensional (3D) by NMR attempted, there will reliance 3D higher dimensional spectroscopy utilizing transfer pathways selective particular constants. The method J doubling suggested increase accuracy measurements large molecules.