Nanosecond Time Scale Motions in Proteins Revealed by High-Resolution NMR Relaxometry

被引:71
|
作者
Charlier, Cyril [1 ]
Khan, Shahid Nawaz [1 ]
Marquardsen, Thorsten [2 ]
Pelupessy, Philippe [1 ]
Reiss, Volker [2 ]
Sakellariou, Dimitris [1 ,3 ]
Bodenhausen, Geoffrey [1 ,4 ]
Engelke, Frank [2 ]
Ferrage, Fabien [1 ]
机构
[1] Ecole Normale Super, Lab Biomol, Dept Chim, CNRS,UPMC,ENS,UMR 7203, F-75231 Paris 05, France
[2] Bruker BioSpin GmbH, D-76287 Rheinstetten, Germany
[3] CEA Saclay, Lab Struct & Dynam Resonance Magnet, CEA, CNRS,IRAMIS,DSM,SIS2M,UMR 3299, F-91191 Gif Sur Yvette, France
[4] Ecole Polytech Fed Lausanne, BCH, Inst Sci & Ingn Chim, CH-1015 Lausanne, Switzerland
基金
欧洲研究理事会;
关键词
MODEL-FREE ANALYSIS; MAGNETIC-RELAXATION DISPERSION; RESIDUAL DIPOLAR COUPLINGS; CROSS-CORRELATION; BACKBONE MOTION; POLARIZATION TRANSFER; CORRELATED MOTIONS; ORDER PARAMETERS; N-15; RELAXATION; SPIN RELAXATION;
D O I
10.1021/ja409820g
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Understanding the molecular determinants underlying protein function requires the characterization of both structure and dynamics at atomic resolution. Nuclear relaxation rates allow a precise characterization of protein dynamics at the Larmor frequencies of spins. This usually limits the sampling of motions to a. narrow range of frequencies corresponding to high magnetic fields. At lower fields one cannot achieve sufficient sensitivity and resolution in NMR Here, we use a fast shuttle device where the polarization builds up and the signals are detected at high field, while longitudinal relaxation takes place at low fields 0.5 < B-0 < 14.1 T. The sample is propelled over a distance up to 50 cm by a blowgun-like system in about 50 ms. The analysis of nitrogen-15 relaxation in the protein ubiquitin over such a wide range of magnetic fields offers unprecedented insights into molecular dynamics. Some key regions of the protein feature structural fluctuations on nanosecond time scales, which have so far been overlooked in high-field relaxation studies. Nanosecond motions in proteins may have been underestimated by traditional high-field approaches, and slower supra-tau(c) motions that have no effect on relaxation may have been overestimated. High-resolution relaxometry thus opens the way to a quantitative characterization of nanosecond motions in proteins.
引用
收藏
页码:18665 / 18672
页数:8
相关论文
共 50 条
  • [21] Capillary HPLC-NMR coupling high-resolution NMR spectroscopy in the nanoliter scale
    Behnke, B
    Schlotterbeck, G
    Tallarek, U
    Strohschein, S
    Tseng, LH
    Keller, T
    Albert, K
    Bayer, E
    ANALYTICAL CHEMISTRY, 1996, 68 (07) : 1110 - 1115
  • [22] Removal of a time barrier for high-resolution multidimensional NMR spectroscopy
    Jaravine V.
    Ibraghimov I.
    Orekhov V.Y.
    Nature Methods, 2006, 3 (8) : 605 - 607
  • [23] Removal of a time barrier for high-resolution multidimensional NMR spectroscopy
    Jaravine, Victor
    Ibraghimov, Ilgis
    Orekhov, Vladislav Yu
    NATURE METHODS, 2006, 3 (08) : 605 - 607
  • [24] High-resolution NMR and ROMP
    Kenwright, AM
    RING OPENING METATHESIS POLYMERISATION AND RELATED CHEMISTRY: STATE OF THE ART AND VISIONS FOR THE NEW CENTURY, 2002, 56 : 57 - 67
  • [25] Pioneers of high-resolution NMR
    Freeman, R
    CONCEPTS IN MAGNETIC RESONANCE, 1999, 11 (02): : 61 - 70
  • [26] HIGH-RESOLUTION ELECTROPHORETIC NMR
    SAARINEN, TR
    JOHNSON, CS
    JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1988, 110 (10) : 3332 - 3333
  • [27] HIGH-RESOLUTION NMR IN SOLIDS
    GRIFFIN, RG
    ANALYTICAL CHEMISTRY, 1977, 49 (11) : A951 - &
  • [28] NMR HIGH-RESOLUTION IN SOLIDS
    STANKOWSKI, J
    PISLEWSKI, N
    IDZIAK, S
    JOURNAL OF MOLECULAR STRUCTURE, 1978, 47 (MAY) : 29 - 39
  • [29] HIGH-RESOLUTION NMR INVIVO
    SHULMAN, RG
    TRENDS IN BIOCHEMICAL SCIENCES, 1988, 13 (02) : 37 - 39
  • [30] HIGH-RESOLUTION NMR IN SOLIDS
    SHINDO, H
    JOURNAL OF SYNTHETIC ORGANIC CHEMISTRY JAPAN, 1981, 39 (07) : 603 - 612