The Magic of Bicelles Lights Up Membrane Protein Structure

被引:280
作者
Duerr, Ulrich H. N. [1 ]
Gildenberg, Melissa [1 ]
Ramamoorthy, Ayyalusamy [1 ]
机构
[1] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA
关键词
SOLID-STATE NMR; RESIDUAL DIPOLAR COUPLINGS; NUCLEAR-MAGNETIC-RESONANCE; ALIGNED PHOSPHOLIPID-BILAYERS; MYELIN BASIC-PROTEIN; ISLET AMYLOID POLYPEPTIDE; HETERONUCLEAR CORRELATION SPECTROSCOPY; ELECTRON-PARAMAGNETIC-RESONANCE; DIMERIC TRANSMEMBRANE DOMAIN; TWIN-ARGININE TRANSLOCASE;
D O I
10.1021/cr300061w
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Biological membranes and membrane proteins, responsible for numerous exciting biological processes, present one of the paramount challenges in biophysics today. Membranes are present in great number and variety in all organisms. They form the boundary between the inside and outside for any bacterium or cell, and they delimit the host of organelles that make up their inner subunits. Membranes delimit any cell and all of its compartments. They form natural borders for metabolic substances and signaling molecules. Membrane proteins are the porters and gatekeepers that make sure that only proper molecules or signals make it across the membrane. The number of elucidated structures of membrane proteins has grown exponentially after the first structure was published in 1985, thus equaling the rate at which structure determination of soluble proteins emerged early on. Still, the number of available high-resolution structures of membrane proteins is limited.
引用
收藏
页码:6054 / 6074
页数:21
相关论文
共 315 条
  • [1] Solid-State NMR Spectroscopy of Membrane-Associated Myelin Basic Protein-Conformation and Dynamics of an Immunodominant Epitope
    Ahmed, Mumdooh A. M.
    Bamm, Vladimir V.
    Harauz, George
    Ladizhansky, Vladimir
    [J]. BIOPHYSICAL JOURNAL, 2010, 99 (04) : 1247 - 1255
  • [2] Residual dipolar couplings: Synergy between NMR and structural genomics
    Al-Hashimi, HM
    Patel, DJ
    [J]. JOURNAL OF BIOMOLECULAR NMR, 2002, 22 (01) : 1 - 8
  • [3] Cell biology - A role for lipid shells in targeting proteins to caveolae, rafts, and other lipid domains
    Anderson, RGW
    Jacobson, K
    [J]. SCIENCE, 2002, 296 (5574) : 1821 - 1825
  • [4] Diffusion and dynamics of penetratin in different membrane mimicking media
    Andersson, A
    Almqvist, J
    Hagn, F
    Mäler, L
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2004, 1661 (01): : 18 - 25
  • [5] The membrane-induced structure of melittin is correlated with the fluidity of the lipids
    Andersson, August
    Biverstahl, Henrik
    Nordin, Jon
    Danielsson, Jens
    Lindahl, Emma
    Maler, Lena
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2007, 1768 (01): : 115 - 121
  • [6] [Anonymous], 2010, UNDERSTANDING NMR SP
  • [7] [Anonymous], 1986, NMR of proteins and nucleic acids
  • [8] Detailed structure and dynamics of bicelle phospholipids using selectively deuterated and perdeuterated labels.: 2H NMR and molecular mechanics study
    Aussenac, F
    Laguerre, M
    Schmitter, JM
    Dufourc, EJ
    [J]. LANGMUIR, 2003, 19 (25) : 10468 - 10479
  • [9] Structure-Dependent Charge Density as a Determinant of Antimicrobial Activity of Peptide Analogues of Defensin
    Bai, Yang
    Liu, Shouping
    Jiang, Ping
    Zhou, Lei
    Li, Jing
    Tang, Charles
    Verma, Chandra
    Mu, Yuguang
    Beuerman, Roger W.
    Pervushin, Konstantin
    [J]. BIOCHEMISTRY, 2009, 48 (30) : 7229 - 7239
  • [10] NMR solution structure and position of transportan in neutral phospholipid bicelles
    Bárány-Wallje, E
    Andersson, A
    Gräslund, A
    Mäler, L
    [J]. FEBS LETTERS, 2004, 567 (2-3): : 265 - 269