Abstract
Natural-abundance nitrogen-15 nuclear magnetic resonance spectroscopy of enzymes and other biopolymers is found to be feasible using newly available instrumentation. The long correlation times of such molecules result in short spin-lattice relaxation times, and these in turn allow rapid signal accumulation. The advantages of short T1 values are sometimes offset, however, by unfavorable nuclear Overhauser effects. The dependence of T1 and nuclear Overhauser effects upon correlation time is discussed, and preliminary nitrogen-15 nuclear magnetic resonance results for several biopolymers, including lysozyme, protamines, pepsin, hemoglobin, vitamin B 12, and tRNA, are presented.
Full text
PDF
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Cozzone P. J., Opella S. J., Jardetzky O., Berthou J., Jollès P. Detection of new temperature-dependent conformational transition in lysozyme by carbon-13 nuclear magnetic resonance spectroscopy. Proc Natl Acad Sci U S A. 1975 Jun;72(6):2095–2098. doi: 10.1073/pnas.72.6.2095. [DOI] [PMC free article] [PubMed] [Google Scholar]
- SOPHIANOPOULOS A. J., RHODES C. K., HOLCOMB D. N., VAN HOLDE K. E. Physical studies of lysozyme. I. Characterization. J Biol Chem. 1962 Apr;237:1107–1112. [PubMed] [Google Scholar]