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Updated: Aug 26, 2025

Myosin-Specific Adaptations of In vitro Fluorescence Microscopy-Based Motility Assays
Published on: February 4, 2021
Myosin head as the main off-odors binding region: Key binding residues and conformational changes in the binding
Chao Xue1, Juan You2, Shanbai Xiong2
1College of Food Science and Technology, and MOE Key Laboratory of Environment Correlative Dietology, Huazhong Agricultural University, Wuhan 430070, China; National R&D Branch Center for Conventional Freshwater Fish Processing, Wuhan 430070, China; Centre for Nutrition and Food Sciences, Queensland Alliance for Agriculture and Food Innovation, The University of Queensland, Brisbane, QLD 4108, Australia.
Abstract:
This study aims to elucidate the dynamic binding characteristics between off-odors (hexanal, 1-octen-3-ol, nonanal) and myosin at cold storage (277 K) and oral temperatures (310 K) through spatial-temporal molecular dynamics (MD) simulation. Conformational analysis indicated that binding with off-odors could not significantly change the myosin secondary structure, and the myosin/(off-odors) structure became a stable and compact state in the later binding stages. Myosin head was the primary binding region with hydrophobic interactions as the dominant force rather than hydrogen bonds (average bond number 202.62 vs 55.20). Furthermore, the myosin/(off-odors) had larger binding energy at 310 than 277 K, and the myosin-nonanal showed the highest binding strength of 4050.93 kJ/mol at 310 K. The binding sites were observed to be concentrated in the 180-249, 350-410, 800-950 amino acid regions of myosin head, especially, Lys185, Tyr347, Leu901. These results provide accurate linkages between off-odors and myosin, laying a theoretical foundation for deodorization of fish products.
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