Krempl, Christina and Sprangers, Remco (2023) Assessing the applicability of <SUP>19</SUP>F labeled tryptophan residues to quantify protein dynamics. JOURNAL OF BIOMOLECULAR NMR, 77 (1-2). pp. 55-67. ISSN 0925-2738, 1573-5001
Full text not available from this repository. (Request a copy)Abstract
Nuclear magnetic resonance (NMR) spectroscopy is uniquely suited to study the dynamics of biomolecules in solution. Most NMR studies exploit the spins of proton, carbon and nitrogen isotopes, as these atoms are highly abundant in proteins and nucleic acids. As an alternative and complementary approach, fluorine atoms can be introduced into biomolecules at specific sites of interest. These labels can then be used as sensitive probes for biomolecular structure, dynamics or interactions. Here, we address if the replacement of tryptophan with 5-fluorotryptophan residues has an effect on the overall dynamics of proteins and if the introduced fluorine probe is able to accurately report on global exchange processes. For the four different model proteins (KIX, Dcp1, Dcp2 and DcpS) that we examined, we established that N-15 CPMG relaxation dispersion or EXSY profiles are not affected by the 5-fluorotryptophan, indicating that this replacement of a proton with a fluorine has no effect on the protein motions. However, we found that the motions that the 5-fluorotryptophan reports on can be significantly faster than the backbone motions. This implies that care needs to be taken when interpreting fluorine relaxation data in terms of global protein motions. In summary, our results underscore the great potential of fluorine NMR methods, but also highlight potential pitfalls that need to be considered.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | RNA DECAPPING ENZYME; NMR-SPECTROSCOPY; KIX DOMAIN; DCP2; INSIGHTS; QUANTIFICATION; RECOGNITION; EQUILIBRIA; EXCHANGE; ENTROPY; Fluorine NMR; Protein dynamics; CPMG relaxation dispersion; Conformational exchange; KIX domain; Dcp1; Dcp2; DcpS; mRNA decapping |
| Subjects: | 500 Science > 530 Physics 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Remco Sprangers |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 07 Mar 2024 14:15 |
| Last Modified: | 07 Mar 2024 14:15 |
| URI: | https://pred.uni-regensburg.de/id/eprint/58928 |
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