| Literature DB >> 34135339 |
Yunbeom Lee1,2, Jong Goo Kim1,2, Sang Jin Lee1,2, Srinivasan Muniyappan1,2, Tae Wu Kim1,2, Hosung Ki1,2, Hanui Kim1,2, Junbeom Jo1,2, So Ri Yun1,2, Hyosub Lee1,2, Kyung Won Lee1,2, Seong Ok Kim1,2, Marco Cammarata3, Hyotcherl Ihee4,5.
Abstract
Ultrafast motion of molecules, particularly the coherent motion, has been intensively investigated as a key factor guiding the reaction pathways. Recently, X-ray free-electron lasers (XFELs) have been utilized to elucidate the ultrafast motion of molecules. However, the studies on proteins using XFELs have been typically limited to the crystalline phase, and proteins in solution have rarely been investigated. Here we applied femtosecond time-resolved X-ray solution scattering (fs-TRXSS) and a structure refinement method to visualize the ultrafast motion of a protein. We succeeded in revealing detailed ultrafast structural changes of homodimeric hemoglobin involving the coherent motion. In addition to the motion of the protein itself, the time-dependent change of electron density of the hydration shell was tracked. Besides, the analysis on the fs-TRXSS data of myoglobin allows for observing the effect of the oligomeric state on the ultrafast coherent motion.Entities:
Mesh：
Substances：
Year: 2021 PMID： 34135339 DOI： 10.1038/s41467-021-23947-7
Source DB: PubMed Journal: Nat Commun ISSN： 2041-1723 Impact factor: 14.919