Biochemistry - How soft is a protein? A protein dynamics force constant measured by neutron scattering

被引:652
作者
Zaccai, G
机构
[1] Inst Biol Struct, F-38027 Grenoble 1, France
[2] Inst Max Von Laue Paul Langevin, F-38042 Grenoble 9, France
关键词
D O I
10.1126/science.288.5471.1604
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
An effective environmental force constant is introduced to quantify the molecular resilience (or its opposite, "softness") of a protein structure and relate it to biological function and activity. Specific resilience-function relations were found in neutron-scattering experiments on purple membranes containing bacteriorhodopsin, the light-activated proton pump of halobacteria; the connection between resilience and stability is illustrated by a study of myoglobin in different environments. Important advantages of the neutron method are that it can characterize the dynamics of any type of biological sample-which need not be crystalline or monodisperse-and that it enables researchers to focus on the dynamics of specific parts of a complex structure with deuterium labeling.
引用
收藏
页码:1604 / 1607
页数:4
相关论文
共 32 条
  • [1] DYNAMICS OF HYDROGEN-ATOMS IN SUPEROXIDE-DISMUTASE BY QUASI-ELASTIC NEUTRON-SCATTERING
    ANDREANI, C
    FILABOZZI, A
    MENZINGER, F
    DESIDERI, A
    DERIU, A
    DICOLA, D
    [J]. BIOPHYSICAL JOURNAL, 1995, 68 (06) : 2519 - 2523
  • [2] Bee M., 1988, QUASIELASTIC NEUTRON
  • [3] Protein, lipid and water organization in bacteriorhodopsin crystals:: a molecular view of the purple membrana at 1.9 Å resolution
    Belrhali, H
    Nollert, P
    Royant, A
    Menzel, C
    Rosenbusch, JP
    Landau, EM
    Pebay-Peyroula, E
    [J]. STRUCTURE, 1999, 7 (08) : 909 - 917
  • [4] PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES
    BERNSTEIN, FC
    KOETZLE, TF
    WILLIAMS, GJB
    MEYER, EF
    BRICE, MD
    RODGERS, JR
    KENNARD, O
    SHIMANOUCHI, T
    TASUMI, M
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1977, 112 (03) : 535 - 542
  • [5] Brooks C. L., 1988, ADV CHEM PHYS, V71, P74
  • [6] Harmonic behavior of trehalose-coated carbon-monoxy-myoglobin at high temperature
    Cordone, L
    Ferrand, M
    Vitrano, E
    Zaccai, G
    [J]. BIOPHYSICAL JOURNAL, 1999, 76 (02) : 1043 - 1047
  • [7] Stability of folded conformations
    Creighton, Thomas E.
    [J]. CURRENT OPINION IN STRUCTURAL BIOLOGY, 1991, 1 (01) : 5 - 16
  • [8] DIPACE A, 1992, BIOPHYS J, V62, P1
  • [9] DYNAMICAL TRANSITION OF MYOGLOBIN REVEALED BY INELASTIC NEUTRON-SCATTERING
    DOSTER, W
    CUSACK, S
    PETRY, W
    [J]. NATURE, 1989, 337 (6209) : 754 - 756
  • [10] THERMAL MOTIONS AND FUNCTION OF BACTERIORHODOPSIN IN PURPLE MEMBRANES - EFFECTS OF TEMPERATURE AND HYDRATION STUDIED BY NEUTRON-SCATTERING
    FERRAND, M
    DIANOUX, AJ
    PETRY, W
    ZACCAI, G
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (20) : 9668 - 9672