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Here, we used bottom-up proteomics and label-free quantification to identify novel post-translational modifications (PTMs) on \u03b2-myosin heavy chain (\u03b2-MHC) in normal and failing human heart tissues. We report six acetylated lysines and two phosphorylated residues: K34-Ac, K58-Ac, S210-P, K213-Ac, T215-P, K429-Ac, K951-Ac, and K1195-Ac. K951-Ac was significantly reduced in both ischemic and nonischemic failing hearts compared to nondiseased hearts. Molecular dynamics (MD) simulations show that K951-Ac may impact stability of thick filament tail interactions and ultimately myosin head positioning. K58-Ac altered the solvent-exposed SH3 domain surface \u2013 known for protein\u2013protein interactions \u2013 but did not appreciably change motor domain conformation or dynamics under conditions studied. Together, K213-Ac\/T215-P altered loop 1\u2019s structure and dynamics \u2013 known to regulate ADP-release, ATPase activity, and sliding velocity. Our study suggests that \u03b2-MHC acetylation levels may be influenced more by the PTM location than the type of heart disease since less protected acetylation sites are reduced in both heart failure groups. Additionally, these PTMs have potential to modulate interactions between \u03b2-MHC and other regulatory sarcomeric proteins, ADP-release rate of myosin, flexibility of the S2 region, and cardiac myofilament contractility in normal and failing hearts.<\/jats:p>","DOI":"10.7554\/elife.74919","type":"journal-article","created":{"date-parts":[[2022,5,3]],"date-time":"2022-05-03T08:00:17Z","timestamp":1651564817000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.74919","source":"Crossref","is-referenced-by-count":24,"title":["Post-translational modification patterns on \u03b2-myosin heavy chain are altered in ischemic and nonischemic human hearts"],"prefix":"10.7554","volume":"11","author":[{"given":"Maicon","family":"Landim-Vieira","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/05g3dte14","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biomedical Sciences, College of Medicine, The Florida State University","place":["Tallahassee, United 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