Peptides are responsible for the regulation of a wide range of physiological functions. Their diverse biological roles, ranging from neurotransmitters to hormones, make them ideal targets for novel drug design. To utilize this potential it is necessary to determine the conformations of these potent bioactive molecules. Nuclear magnetic resonance spectroscopy provides a means for determining conformations of peptide species, both free in solution and, in appropriate cases, when bound to their receptors. In this article, NMR-based methods for determining conformations of bioactive peptides are described and illusrated with specific examples. This includes a discussion of qualitative and quantitative methods for assessment of NMR data, as well as methods used to investigate dynamics.
|Number of pages||30|
|Journal||Current Medicinal Chemistry|
|Publication status||Published - 1 Dec 1994|