caa a22 4500 445325305 CHVBK 20180317142718.0 cr unu---uuuuu 170323e20111101xx s 000 0 eng 10.1007/s10858-011-9535-z doi (NATIONALLICENCE)springer-10.1007/s10858-011-9535-z Cryogenic temperature effects and resolution upon slow cooling of protein preparations in solid state NMR [Elektronische Daten] [Arne Linden, W. Franks, Ümit Akbey, Sascha Lange, Barth-Jan van Rossum, Hartmut Oschkinat] X-ray crystallography using synchrotron radiation and the technique of dynamic nuclear polarization (DNP) in nuclear magnetic resonance (NMR) require samples to be kept at temperatures below 100K. Protein dynamics are poorly understood below the freezing point of water and down to liquid nitrogen temperatures. Therefore, we investigate the α-spectrin SH3 domain by magic angle spinning (MAS) solid state NMR (ssNMR) at various temperatures while cooling slowly. Cooling down to 95K, the NMR-signals of SH3 first broaden and at lower temperatures they separate into several peaks. The coalescence temperature differs depending on the individual residue. The broadening is shown to be inhomogeneous by hole-burning experiments. The coalescence behavior of 26 resolved signals (of 62) was compared to water proximity and crystal structure Debye-Waller factors (B-factors). Close proximity to the solvent and large B-factors (i.e. mobility) lead, generally, to a higher coalescence temperature. We interpret a high coalescence temperature as indicative of a large number of magnetically inequivalent populations at cryogenic temperature. Springer Science+Business Media B.V., 2011 Cryogenic NMR spectroscopy nationallicence Low-temperature dynamics nationallicence Solvent effects nationallicence Protein glass transition nationallicence Coalescence nationallicence Linden Arne Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut Franks W. Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut Akbey Ümit Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut Lange Sascha Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut van Rossum Barth-Jan Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut Oschkinat Hartmut Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 283-292 0925-2738 51:3<283 2011 51 10858 https://doi.org/10.1007/s10858-011-9535-z text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10858-011-9535-z text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Linden Arne Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut NATIONALLICENCE 700 1- Franks W. Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut NATIONALLICENCE 700 1- Akbey Ümit Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut NATIONALLICENCE 700 1- Lange Sascha Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut NATIONALLICENCE 700 1- van Rossum Barth-Jan Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut NATIONALLICENCE 700 1- Oschkinat Hartmut Forschungsinstitut für Molekulare Pharmakologie (FMP), Robert-Rössle-Straße 10, 13125, Berlin, Germany aut NATIONALLICENCE 773 0- Journal of Biomolecular NMR Springer Netherlands 51/3(2011-11-01), 283-292 0925-2738 51:3<283 2011 51 10858 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer