caa a22 4500 445325933 CHVBK 20180317142720.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s10858-011-9500-x doi (NATIONALLICENCE)springer-10.1007/s10858-011-9500-x Temperature dependence of fast carbonyl backbone dynamics in chicken villin headpiece subdomain [Elektronische Daten] [Liliya Vugmeyster, Dmitry Ostrovsky] Temperature-dependence of protein dynamics can provide information on details of the free energy landscape by probing the characteristics of the potential responsible for the fluctuations. We have investigated the temperature-dependence of picosecond to nanosecond backbone dynamics at carbonyl carbon sites in chicken villin headpiece subdomain protein using a combination of three NMR relaxation rates: 13C′ longitudinal rate, and two cross-correlated rates involving dipolar and chemical shift anisotropy (CSA) relaxation mechanisms, 13C′/13C′-13Cα CSA/dipolar and 13C′/13C′-15N CSA/dipolar. Order parameters have been extracted using the Lipari-Szabo model-free approach assuming a separation of the time scales of internal and molecular motions in the 2-16°C temperature range. There is a gradual deviation from this assumption from lower to higher temperatures, such that above 16°C the separation of the time scales is inconsistent with the experimental data and, thus, the Lipari-Szabo formalism can not be applied. While there are variations among the residues, on the average the order parameters indicate a markedly steeper temperature dependence at backbone carbonyl carbons compared to that probed at amide nitrogens in an earlier study. This strongly advocates for probing sites other than amide nitrogen for accurate characterization of the potential and other thermodynamics characteristics of protein backbone. Springer Science+Business Media B.V., 2011 Protein dynamics nationallicence Temperature-dependence nationallicence Model-free nationallicence Chicken villin headpiece nationallicence NMR relaxation nationallicence Vugmeyster Liliya Department of Chemistry and Environment and Natural Resources Institute, University of Alaska at Anchorage, 3211 Providence Drive, 99508, Anchorage, AK, USA aut Ostrovsky Dmitry Department of Mathematical Sciences, University of Alaska at Anchorage, 3211 Providence Drive, 99508, Anchorage, AK, USA aut Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 119-127 0925-2738 50:2<119 2011 50 10858 https://doi.org/10.1007/s10858-011-9500-x text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9500-x text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Vugmeyster Liliya Department of Chemistry and Environment and Natural Resources Institute, University of Alaska at Anchorage, 3211 Providence Drive, 99508, Anchorage, AK, USA aut NATIONALLICENCE 700 1- Ostrovsky Dmitry Department of Mathematical Sciences, University of Alaska at Anchorage, 3211 Providence Drive, 99508, Anchorage, AK, USA aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 50/2(2011-06-01), 119-127 0925-2738 50:2<119 2011 50 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer