Experimental and computational characterization of biological liquid crystals: a review of single-molecule bioassays.
Quantitative understanding of the mechanical behavior of biological liquid crystals such as proteins is essential for gaining insight into their biological functions, since some proteins perform notable mechanical functions. Recently, single-molecule experiments have allowed not only the quantitative characterization of the mechanical behavior of proteins such as protein unfolding mechanics, but also the exploration of the free energy landscape for protein folding. In this work, we have reviewed the current state-of-art in single-molecule bioassays that enable quantitative studies on protein unfolding mechanics and/or various molecular interactions. Specifically, single-molecule pulling experiments based on atomic force microscopy (AFM) have been overviewed. In addition, the computational simulations on single-molecule pulling experiments have been reviewed. We have also reviewed the AFM cantilever-based bioassay that provides insight into various molecular interactions. Our review highlights the AFM-based single-molecule bioassay for quantitative characterization of biological liquid crystals such as proteins.
Eom
Kilho
K
Department of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Yang
Jaemoon
J
Department of Radiology, College of Medicine, Yonsei University, Seoul 120-752, Korea.
Park
Jinsung
J
Department of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Yoon
Gwonchan
G
Department of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Sohn
Young Soo
YS
Department of Biomedical Engineering, Catholic University of Daegu, Kyeongbuk 712-702, Korea.
Park
Shinsuk
S
Department of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Yoon
Dae Sung
DS
Department of Biomedical Engineering, Yonsei University, Kangwon-do 220-740, Korea.
Na
Sungsoo
S
Department of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Kwon
Taeyun
T
Research Institute of Engineering and Technology, Korea University, Seoul 136-701, Korea.
D001696:Biomechanical Phenomena; D006860:Hydrogen Bonding; D050866:Liquid Crystals / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D008956:Models, Chemical; D056004:Molecular Dynamics Simulation; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry; D013816:Thermodynamics
D011506:Proteins