Abstract：
: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.
journal_name
Int J Mol Scijournal_title
International journal of molecular sciencesauthors
Eom K,Yang J,Park J,Yoon G,Soo Sohn Y,Park S,Yoon DS,Na S,Kwon Tdoi
10.3390/ijms10094009subject
Has Abstractpub_date
2009-09-10 00:00:00pages
4009-32issue
9issn
1422-0067journal_volume
10pub_type
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