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
  • [21] Spatial Structure and pH-dependent Conformational Diversity of Dimeric Transmembrane Domain of the Receptor Tyrosine Kinase EphA1
    Bocharov, Eduard V.
    Mayzel, Maxim L.
    Volynsky, Pavel E.
    Goncharuk, Marina V.
    Ermolyuk, Yaroslav S.
    Schulga, Alexey A.
    Artemenko, Elena O.
    Efremov, Roman G.
    Arseniev, Alexander S.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (43) : 29385 - 29395
  • [22] Spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 presumably corresponding to the receptor active state
    Bocharov, Eduard V.
    Mineev, Konstantin S.
    Volynsky, Pavel E.
    Ermolyuk, Yaroslav S.
    Tkach, Elena N.
    Sobol, Alexander G.
    Chupin, Vladimir V.
    Kirpichnikov, Michail P.
    Efremov, Roman G.
    Arseniev, Alexander S.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2008, 283 (11) : 6950 - 6956
  • [23] Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger
    Bocharov, Eduard V.
    Pustovalova, Yulia E.
    Pavlov, Konstantin V.
    Volynsky, Pavel E.
    Goncharuk, Marina V.
    Ermolyuk, Yaroslav S.
    Karpunin, Dmitry V.
    Schulga, Alexey A.
    Kirpichnikov, Michail P.
    Efremov, Roman G.
    Maslennikov, Innokenty V.
    Arseniev, Alexander S.
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (22) : 16256 - 16266
  • [24] Structural and thermodynamic insight into the process of "weak" dimerization of the ErbB4 transmembrane domain by solution NMR
    Bocharov, Eduard V.
    Mineev, Konstantin S.
    Goncharuk, Marina V.
    Arseniev, Alexander S.
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2012, 1818 (09): : 2158 - 2170
  • [25] Structure elucidation of dimeric transmembrane domains of bitopic proteins
    Bocharov, Eduard V.
    Volynsky, Pavel E.
    Pavlov, Konstantin V.
    Efremov, Roman G.
    Arseniev, Alexander S.
    [J]. CELL ADHESION & MIGRATION, 2010, 4 (02) : 284 - 298
  • [26] NMR analysis of protein interactions
    Bonvin, AMJJ
    Boelens, R
    Kaptein, R
    [J]. CURRENT OPINION IN CHEMICAL BIOLOGY, 2005, 9 (05) : 501 - 508
  • [27] Evidence that bilayer bending rigidity affects membrane protein folding
    Booth, PJ
    Riley, ML
    Flitsch, SL
    Templer, RH
    Farooq, A
    Curran, AR
    Chadborn, N
    Wright, P
    [J]. BIOCHEMISTRY, 1997, 36 (01) : 197 - 203
  • [28] Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplings
    Bouvignies, Guillaume
    Markwick, Phineus R. L.
    Blackledge, Martin
    [J]. CHEMPHYSCHEM, 2007, 8 (13) : 1901 - 1909
  • [29] Membrane fragmentation by an amyloidogenic fragment of human Islet Amyloid Polypeptide detected by solid-state NMR spectroscopy of membrane nanotubes
    Brender, Jeffrey R.
    Duerr, Ulrich H. N.
    Heyl, Deborah
    Budarapu, Mahender B.
    Ramamoorthy, Ayyalusamy
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2007, 1768 (09): : 2026 - 2029
  • [30] Membrane Disruption and Early Events in the Aggregation of the Diabetes Related Peptide IAPP from a Molecular Perspective
    Brender, Jeffrey R.
    Salamekh, Samer
    Ramamoorthy, Ayyalusamy
    [J]. ACCOUNTS OF CHEMICAL RESEARCH, 2012, 45 (03) : 454 - 462