| Literature DB >> 31576526 |
Christina I Schroeder1, K Johan Rosengren2.
Abstract
Nuclear magnetic resonance (NMR) spectroscopy has over the last few decades proven to be an extremely useful technique for, and indeed an integral part of, investigating the structural features of peptides and small proteins directly in solution, without the need for crystallization. This advantage over X-ray methods is important when dealing with peptides and small proteins that do not readily form crystals. In this chapter we outline what specific NMR experiments are useful, considerations about how to acquire and interpret these experiments, and how information derived from the NMR data can be used to determine solution structures of small peptides.Keywords: Homonuclear NMR; Nuclear Magnetic Resonance spectroscopy; Nuclear Overhauser effect spectroscopy; Peptide; Total correlation spectroscopy
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Year: 2020 PMID: 31576526 DOI: 10.1007/978-1-4939-9845-6_7
Source DB: PubMed Journal: Methods Mol Biol ISSN: 1064-3745