## Abstract The equilibrium between the __cis__ and __trans__ forms of XβPro peptide bonds can readily be measured in the ^13^C nmr spectra. In the present paper we investigate how observation of this equilibrium could be used as an nmr probe for conformational studies of flexible polypeptide chain
Fluorine as an NMR probe for structural studies of chemical and biological systems
β Scribed by Yelena G. Gakh; Andrei A. Gakh; Angela M. Gronenborn
- Publisher
- John Wiley and Sons
- Year
- 2000
- Tongue
- English
- Weight
- 137 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0749-1581
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β¦ Synopsis
Applications of fluorine NMR to probe long-range interactions in rigid organic molecules, namely cubanes, and to study structures and dynamics of proteins and other biological systems, are presented. F NMR parameters, especially long-range coupling constants are shown to reveal intrinsic features of the molecules. Correlations between long-range (more than three-bond) couplings involving fluorine and other chemical and physicochemical properties of the compounds are demonstrated, and examples of unusual couplings which cannot be explained by existing theories of 'through-bond' and 'through-space' mechanisms are discussed. Recent applications of fluorine labeling of aromatic and aliphatic amino acids in investigating protein structures and dynamics are highlighted. The potential of using 19 F NMR parameters, such as large spin-spin coupling constants observed for organic compounds, for structural analysis of biological macromolecules is outlined.
π SIMILAR VOLUMES
We describe the construction of an NMR probe and cell chamber with good mixing, pH buffering, and oxygenation characteristics, which can be used for relatively dilute cell and organelle suspensions. The "P NMR spectra of acceptable signal-to-noise ratios are obtained from approximately 200 mg (prote