Products Cited in Publications Worldwide Spatially confined protein assembly in hierarchical mesoporous metal-organic framework

Spatially confined protein assembly in hierarchical mesoporous metal-organic framework

Wang, Xiaoliang; He, Lilin; Sumner, Jacob; Qian, Shuo; Zhang, Qiu; O′Neill, Hugh; Mao, Yimin; Chen, Chengxia; Al-Enizi, Abdullah M.; Nafady, Ayman; Ma, Shengqian

DOI: PMID:

Abstract

Immobilization of biomols. into porous materials could lead to significantly enhanced performance in terms of stability towards harsh reaction conditions and easier separation for their reuse. Metal-Organic Frameworks (MOFs), offering unique structural features, have emerged as a promising platform for immobilizing large biomols. Although many indirect methods have been used to investigate the immobilized biomols. for diverse applications, understanding their spatial arrangement in the pores of MOFs is still preliminary due to the difficulties in directly monitoring their conformations. To gain insights into the spatial arrangement of biomols. within the nanopores. We used in situ small-angle neutron scattering (SANS) to probe deuterated green fluorescent protein (d-GFP) entrapped in a mesoporous MOF. Our work revealed that GFP mols. are spatially arranged in adjacent nanosized cavities of MOF-919 to form "assembly" through adsorbate-adsorbate interactions across pore apertures. Our findings, therefore, lay a crucial foundation for the identification of proteins structural basics under confinement environment of MOFs.

Purchased from AmBeed

4-Carboxypyrazole

A11806037718-11-998%

4-Carboxypyrazole

15.0/10g

Detail