caa a22 4500 47713632X CHVBK 20180405111719.0 cr unu---uuuuu 170330e19970101xx s 000 0 eng 10.1023/A:1018675618785 doi (NATIONALLICENCE)springer-10.1023/A:1018675618785 Backbone dynamics of proteins derived from carbonyl carbon relaxation times at 500, 600 and 800 MHz: Application to ribonuclease T1 [Elektronische Daten] [Jan Engelke, Heinz Rüterjans] The backbone dynamics of uniformly 13C/15N-enriched ribonuclease T1 have beeninvestigated using carbonyl carbon relaxation times recorded at three different spectrometerfrequencies. Pulse sequences for the determination of the longitudinal (T1) and transverse (T2)relaxation times are presented. The relaxation behaviour was analysed in terms of a multispinsystem. Although the chemical shift anisotropy relaxation mechanism dominates at highmagnetic field strength, the contributions of the dipole-dipole interactions and thecross-correlation between these two relaxation mechanisms have also been considered.Information about internal motions has been extracted from the relaxation data using themodel-free approach of Lipari and Szabo in order to determine order parameters (S2) andeffective internal correlation times (τi). Using a relatively simple relation between themeasured relaxation rates and the spectral density function, an analytical expression for themicrodynamical parameters in dependence of T1 and T2 has been derived. The spectraldensity mapping technique has been applied in order to study the behaviour of the carbonylcarbon resonances in more detail. Kluwer Academic Publishers, 1997 Protein dynamics nationallicence 13C relaxation times nationallicence Spectral density function mapping nationallicence Conformational exchange nationallicence Order parameter nationallicence Ribonuclease T1 nationallicence Engelke Jan Institut für Biophysikalische Chemie der Johann Wolfgang Goethe Universität, Frankfurt am Main, Biozentrum N230, Marie Curie Strasse 9, D-60439, Frankfurt am Main, Germany aut Rüterjans Heinz Institut für Biophysikalische Chemie der Johann Wolfgang Goethe Universität, Frankfurt am Main, Biozentrum N230, Marie Curie Strasse 9, D-60439, Frankfurt am Main, Germany aut Journal of Biomolecular NMR Kluwer Academic Publishers 9/1(1997-01-01), 63-78 0925-2738 9:1<63 1997 9 10858 https://doi.org/10.1023/A:1018675618785 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1023/A:1018675618785 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Engelke Jan Institut für Biophysikalische Chemie der Johann Wolfgang Goethe Universität, Frankfurt am Main, Biozentrum N230, Marie Curie Strasse 9, D-60439, Frankfurt am Main, Germany aut NATIONALLICENCE 700 1- Rüterjans Heinz Institut für Biophysikalische Chemie der Johann Wolfgang Goethe Universität, Frankfurt am Main, Biozentrum N230, Marie Curie Strasse 9, D-60439, Frankfurt am Main, Germany aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Kluwer Academic Publishers 9/1(1997-01-01), 63-78 0925-2738 9:1<63 1997 9 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer