Temperature-dependent spectral density analysis applied to monitoring backbone dynamics of major urinary protein-I complexed with the pheromone 2-sec-buty1-4, 5-dihydrothiazole

Hana Křížová, Lukáš Žídek, Martin J. Stone, Milos V. Novotny, Vladimír Sklenář

Research output: Contribution to journalArticleResearchpeer-review

47 Citations (Scopus)


Backbone dynamics of mouse major urinary protein I (MUP-I) was studied by 15N NMR relaxation. Data were collected at multiple temperatures for a complex of MUP-I with its natural pheromonal ligand, 2-sec-4,5-dihydrothiazole, and for the free protein. The measured relaxation rates were analyzed using the reduced spectral density mapping. Graphical analysis of the spectral density values provided an unbiased qualitative picture of the internal motions. Varying temperature greatly increased the range of analyzed spectral density values and therefore improved reliability of the analysis. Quantitative parameters describing the dynamics on picosecond to nanosecond time scale were obtained using a novel method of simultaneous data fitting at multiple temperatures. Both methods showed that the backbone flexibility on the fast time scale is slightly increased upon pheromone binding, in accordance with the previously reported results. Zero-frequency spectral density values revealed conformational changes on the microsecond to millisecond time scale. Measurements at different temperatures allowed to monitor temperature depencence of the motional parameters.

Original languageEnglish
Pages (from-to)369-384
Number of pages16
JournalJournal of Biomolecular NMR
Issue number4
Publication statusPublished - Apr 2004
Externally publishedYes


  • Backbone dynamics
  • NMR relaxation
  • Spectral density function
  • Temperature dependence

Cite this