Cross-saturation and transferred cross-saturation experiments

摘要

since the structure itself yields few clues about the specific targetrecognition. Therefore, structural analyses of protein–protein interactions are required to reveal the mechanism of their functions. Several attempts have been made to investigate protein–protein interactions by using NMR [1–5]. Especially, NMR methods that use chemical shift perturbation [6] and/or hydrogen–deuterium (H–D) exchange [7] for the main-chain amide groups of the complex have frequently been used to identify the interfaces of larger protein–protein complexes with molecular mass of over 50 kDa in solution.