Title:NMR Spectroscopy in the Conformational Analysis of Peptides: An Overview
Volume: 28
Issue: 14
关键词:
核磁共振、结构生物学、肽、蛋白质、构象集合、距离和角度限制、生物活性构象。
摘要:
Background: NMR spectroscopy is one of the most powerful tools to study the
structure and interaction properties of peptides and proteins from a dynamic perspective.
Knowing the bioactive conformations of peptides is crucial in the drug discovery field to design
more efficient analogue ligands and inhibitors of protein-protein interactions targeting
therapeutically relevant systems.
Objective: This review provides a toolkit to investigate peptide conformational properties by
NMR.
Methods: Articles cited herein, related to NMR studies of peptides and proteins were mainly
searched through PubMed and the web. More recent and old books on NMR spectroscopy
written by eminent scientists in the field were consulted as well.
Results: The review is mainly focused on NMR tools to gain the 3D structure of small unlabeled
peptides. It is more application-oriented as it is beyond its goal to deliver a profound
theoretical background. However, the basic principles of 2D homonuclear and heteronuclear
experiments are briefly described. Protocols to obtain isotopically labeled peptides and principal
triple resonance experiments needed to study them, are discussed as well.
Conclusion: NMR is a leading technique in the study of conformational preferences of small
flexible peptides whose structure can be often only described by an ensemble of conformations.
Although NMR studies of peptides can be easily and fast performed by canonical protocols
established a few decades ago, more recently we have assisted to tremendous improvements
of NMR spectroscopy to investigate instead large systems and overcome its molecular
weight limit.