Analytical ultracentrifugation: A versatile tool for the characterisation of macromolecular complexes in solution

被引:24
作者
Patel, Trushar R. [1 ]
Winzor, Donald J. [2 ]
Scott, David J. [3 ,4 ,5 ]
机构
[1] Univ Birmingham, Sch Biosci, Birmingham B15 2TT, W Midlands, England
[2] Univ Queensland, Sch Chem & Mol Biosci, Brisbane, Qld 4072, Australia
[3] Univ Nottingham, Sch Biosci, Natl Ctr Macromol Hydrodynam, Sutton Bonington Campus, Loughborough LE12 5RD, Leics, England
[4] ISIS Spallat Neutron & Muon Source, Oxford OX11 0FA, Oxon, England
[5] Rutherford Appleton Lab, Res Complex Harwell, Oxford OX11 0FA, Oxon, England
基金
英国生物技术与生命科学研究理事会;
关键词
Analytical ultracentrifugation; Catalytic complex in selenocysteine synthesis; Cytoplasmic dynein complex; Mitogen-activated protein kinase (ERK2); Sedimentation equilibrium; Sedimentation velocity; SepSecS-tRNA(sec) interaction; MAP KINASE ERK2; SEDIMENTATION-VELOCITY; PHYSICOCHEMICAL EVIDENCE; INTERACTING SUBSTANCES; CYTOPLASMIC DYNEIN; BOUNDARY ANALYSIS; PROTEIN; SELENOCYSTEINE; BRAIN; PHOSPHORYLATION;
D O I
10.1016/j.ymeth.2015.11.006
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Analytical ultracentrifugation, an early technique developed for characterizing quantitatively the solution properties of macromolecules, remains a powerful aid to structural biologists in their quest to understand the formation of biologically important protein complexes at the molecular level. Treatment of the basic tenets of the sedimentation velocity and sedimentation equilibrium variants of analytical ultracentrifugation is followed by considerations of the roles that it, in conjunction with other physicochemical procedures, has played in resolving problems encountered in the delineation of complex formation for three biological systems - the cytoplasmic dynein complex, mitogen-activated protein kinase (ERK2) self-interaction, and the terminal catalytic complex in selenocysteine synthesis. (C) 2015 Elsevier Inc. All rights reserved.
引用
收藏
页码:55 / 61
页数:7
相关论文
共 60 条
  • [1] ADAMS ET, 1963, ULTRACENTRIFUGAL ANA, P119
  • [3] The channel-forming protein proaerolysin remains a dimer at low concentrations in solution
    Barry, R
    Moore, S
    Alonso, A
    Ausió, J
    Buckley, JT
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (01) : 551 - 554
  • [4] Properties and regulation of a transiently assembled ERK2•Ets-1 signaling complex
    Callaway, Kari A.
    Rainey, Mark A.
    Riggs, Austen F.
    Abramczyk, Olga
    Dalby, Kevin N.
    [J]. BIOCHEMISTRY, 2006, 45 (46) : 13719 - 13733
  • [5] Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
    Canagarajah, BJ
    Khokhlatchev, A
    Cobb, MH
    Goldsmith, EJ
    [J]. CELL, 1997, 90 (05) : 859 - 869
  • [6] Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    de la Torre, JG
    Huertas, ML
    Carrasco, B
    [J]. BIOPHYSICAL JOURNAL, 2000, 78 (02) : 719 - 730
  • [7] Sedimentation velocity analysis of highly heterogeneous systems
    Demeler, B
    van Holde, KE
    [J]. ANALYTICAL BIOCHEMISTRY, 2004, 335 (02) : 279 - 288
  • [8] Demeler B, 2005, ANALYTICAL ULTRACENTRIFUGATION: TECHNIQUES AND METHODS, P210
  • [9] Characterization of Reversible Associations by Sedimentation Velocity with UltraScan
    Demeler, Borries
    Brookes, Emre
    Wang, Renjing
    Schirf, Virgil
    Kim, Chongwoo A.
    [J]. MACROMOLECULAR BIOSCIENCE, 2010, 10 (07) : 775 - 782
  • [10] Transport and egress of herpes simplex virus in neurons
    Diefenbach, Russell J.
    Miranda-Saksena, Monica
    Douglas, Mark W.
    Cunningham, Anthony L.
    [J]. REVIEWS IN MEDICAL VIROLOGY, 2008, 18 (01) : 35 - 51