High-speed atomic force microscopy: Structure and dynamics of single proteins

被引:27
作者
Casuso, Ignacio [1 ]
Rico, Felix [1 ]
Scheuring, Simon [1 ]
机构
[1] INSERM, Inst Curie, U1006, F-75005 Paris, France
关键词
MYOSIN-V; NANO-VISUALIZATION; RESOLUTION; TITIN; AFM;
D O I
10.1016/j.cbpa.2011.05.007
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
For surface analysis of biological molecules, atomic force microscopy (AFM) is an appealing technique combining data acquisition under physiological conditions, for example buffer solution, room temperature and ambient pressure, and high resolution. However, a key feature of life, dynamics, could not be assessed until recently because of the slowness of conventional AFM setups. Thus, for observing bio-molecular processes, the gain of image acquisition speed signifies a key progress. Here, we review the development and recent achievements using high-speed atomic force microscopy (HS-AFM). The HS-AFM is now the only technique to assess structure and dynamics of single molecules, revealing molecular motor action and diffusion dynamics. From this imaging data, watching molecules at work, novel and direct insights could be gained concerning the structure, dynamics and function relationship at the single bio-molecule level.
引用
收藏
页码:704 / 709
页数:6
相关论文
共 42 条
[1]   A high-speed atomic force microscope for studying biological macromolecules [J].
Ando, T ;
Kodera, N ;
Takai, E ;
Maruyama, D ;
Saito, K ;
Toda, A .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (22) :12468-12472
[2]   High-speed AFM and nano-visualization of biomolecular processes [J].
Ando, Toshio ;
Uchihashi, Takayuki ;
Kodera, Noriyuki ;
Yamamoto, Daisuke ;
Miyagi, Atsushi ;
Taniguchi, Masaaki ;
Yamashita, Hayato .
PFLUGERS ARCHIV-EUROPEAN JOURNAL OF PHYSIOLOGY, 2008, 456 (01) :211-225
[3]   High-speed atomic force microscopy for nano-visualization of dynamic biomolecular processes [J].
Ando, Toshio ;
Uchihashi, Takayuki ;
Fukuma, Takeshi .
PROGRESS IN SURFACE SCIENCE, 2008, 83 (7-9) :337-437
[4]   MOBILITY MEASUREMENT BY ANALYSIS OF FLUORESCENCE PHOTOBLEACHING RECOVERY KINETICS [J].
AXELROD, D ;
KOPPEL, DE ;
SCHLESSINGER, J ;
ELSON, E ;
WEBB, WW .
BIOPHYSICAL JOURNAL, 1976, 16 (09) :1055-1069
[5]   Membrane lateral diffusion and capture of CFTR within transient confinement zones [J].
Bates, Ian R. ;
Hebert, Benedict ;
Luo, Yishan ;
Liao, Jie ;
Bachir, Alexia I. ;
Kolin, David L. ;
Wiseman, Paul W. ;
Hanrahan, John W. .
BIOPHYSICAL JOURNAL, 2006, 91 (03) :1046-1058
[6]   ATOMIC FORCE MICROSCOPE [J].
BINNIG, G ;
QUATE, CF ;
GERBER, C .
PHYSICAL REVIEW LETTERS, 1986, 56 (09) :930-933
[7]   ATOMIC RESOLUTION WITH ATOMIC FORCE MICROSCOPE [J].
BINNIG, G ;
GERBER, C ;
STOLL, E ;
ALBRECHT, TR ;
QUATE, CF .
EUROPHYSICS LETTERS, 1987, 3 (12) :1281-1286
[8]   Myosin V stepping mechanism [J].
Cappello, Giovanni ;
Pierobon, Paolo ;
Symonds, Clementine ;
Busoni, Lorenzo ;
Gebhardt, J. Christof M. ;
Rief, Matthias ;
Prost, Jacques .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2007, 104 (39) :15328-15333
[9]  
CASUSO I, COMPLETE LATER UNPUB
[10]   Experimental Evidence for Membrane-Mediated Protein-Protein Interaction [J].
Casuso, Ignacio ;
Sens, Pierre ;
Rico, Felix ;
Scheuring, Simon .
BIOPHYSICAL JOURNAL, 2010, 99 (07) :L47-L49