Allosteric Switching of Calmodulin in a Mycobacterium smegmatis porin A (MspA) Nanopore‐Trap

Recent developments concerning large protein nanopores suggest a new approach to structure profiling of native folded proteins. In this work, the large vestibule of Mycobacterium smegmatis porin A (MspA) and calmodulin (CaM), a Ca2+‐binding protein, were used in the direct observation of the protein...

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Veröffentlicht in:	Angewandte Chemie International Edition 2021-10, Vol.60 (44), p.23863-23870
Hauptverfasser:	Liu, Yao, Pan, Tiezheng, Wang, Kefan, Wang, Yuqin, Yan, Shuanghong, Wang, Liying, Zhang, Shanyu, Du, Xiaoyu, Jia, Wendong, Zhang, Panke, Chen, Hong‐Yuan, Huang, Shuo
Format:	Artikel
Sprache:	eng
Schlagworte:	Allosteric properties Allosteric Regulation Amino acids Calcium ions Calcium-binding protein Calmodulin Calmodulin - metabolism Lead Magnesium Mycobacterium smegmatis Mycobacterium smegmatis - metabolism Mycobacterium smegmatis porin A nanopore-traps Porins - metabolism protein allosterism Protein structure Proteins single-molecule studies Stability analysis Vestibules
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