From valleys to ridges:: Exploring the dynamic energy landscape of single membrane proteins

被引:41
作者
Janovjak, Harald [2 ]
Sapra, K. Tanuj [1 ]
Kedrov, Alexej [1 ]
Mueller, Daniel J. [1 ]
机构
[1] Tech Univ Dresden, Ctr Biotechnol, Dept Cellular Machines, D-01307 Dresden, Germany
[2] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
关键词
atomic force microscopy; molecular interactions; protein folding; kinetics; single-molecule studies;
D O I
10.1002/cphc.200700662
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
Membrane proteins are involved in essential biological processes such as energy conversion, signal transduction, solute transport and secretion. All biological processes, also those involving membrane proteins, are steered by molecular interactions. Molecular interactions guide the folding and stability of membrane proteins, determine their assembly, switch their functional states or mediate signal transduction. The sequential steps of molecular interactions driving these processes con be described by dynamic energy landscapes. The conceptual energy landscape allows to follow the complex reaction pathways of membrane proteins while its modifications describe why and how pathways ore changed. Single-molecule force spectroscopy (SMFS) detects, quantifies and locates interactions within and between membrane proteins. SMFS helps to determine how these interactions change with temperature, point mutations, oligomerization and the functional states of membrane proteins. Applied in different modes, SMFS explores the co-existence and population of reaction pathways in the energy landscape of the protein and thus reveals detailed insights into local mechanisms, determining its structural and functional relationships. Here we review how SMFS extracts the defining parameters of an energy landscape such as the barrier position, reaction kinetics and roughness with high precision.
引用
收藏
页码:954 / 966
页数:13
相关论文
共 134 条
[91]   Direct measurement of protein energy landscape roughness [J].
Nevo, R ;
Brumfeld, V ;
Kapon, R ;
Hinterdorfer, P ;
Reich, Z .
EMBO REPORTS, 2005, 6 (05) :482-486
[92]   Unfolding pathways of individual bacteriorhodopsins [J].
Oesterhelt, F ;
Oesterhelt, D ;
Pfeiffer, M ;
Engel, A ;
Gaub, HE ;
Müller, DJ .
SCIENCE, 2000, 288 (5463) :143-146
[93]   Folding and binding - The conformational repertoire of proteins: folding, aggregation and structural recognition [J].
Oliveberg, M ;
Shakhnovich, EI .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2006, 16 (01) :68-70
[94]   The experimental survey of protein-folding energy landscapes [J].
Oliveberg, Mikael ;
Wolynes, Peter G. .
QUARTERLY REVIEWS OF BIOPHYSICS, 2005, 38 (03) :245-288
[95]   Theory of protein folding [J].
Onuchic, JN ;
Wolynes, PG .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 2004, 14 (01) :70-75
[96]   TOWARD AN OUTLINE OF THE TOPOGRAPHY OF A REALISTIC PROTEIN-FOLDING FUNNEL [J].
ONUCHIC, JN ;
WOLYNES, PG ;
LUTHEYSCHULTEN, Z ;
SOCCI, ND .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (08) :3626-3630
[97]   Crystal structure of rhodopsin: A G protein-coupled receptor [J].
Palczewski, K ;
Kumasaka, T ;
Hori, T ;
Behnke, CA ;
Motoshima, H ;
Fox, BA ;
Le Trong, I ;
Teller, DC ;
Okada, T ;
Stenkamp, RE ;
Yamamoto, M ;
Miyano, M .
SCIENCE, 2000, 289 (5480) :739-745
[98]   Stabilizing effect of Zn2+ in native bovine rhodopsin [J].
Park, Paul S. -H. ;
Sapra, K. Tanuj ;
Kolinski, Michal ;
Filipek, Slawomir ;
Palczewski, Krzysztof ;
Muller, Daniel J. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (15) :11377-11385
[99]   Protein unfolding in the cell [J].
Prakash, S ;
Matouschek, A .
TRENDS IN BIOCHEMICAL SCIENCES, 2004, 29 (11) :593-600
[100]   Free energy of membrane protein unfolding derived from single-molecule force measurements [J].
Preiner, Johannes ;
Janovjak, Harald ;
Rankl, Christian ;
Knaus, Helene ;
Cisneros, David A. ;
Kedrov, Alexej ;
Kienberger, Ferry ;
Muller, Daniel J. ;
Hinterdorfer, Peter .
BIOPHYSICAL JOURNAL, 2007, 93 (03) :930-937