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Lysine acetylation of F-actin decreases tropomyosin-based inhibition of actomyosin activity

ABSTRACT: Actin was acetylated on lysine residues with acetic anhydride to determine its impaction on the contractile properties of the thin filaments including, actin's ability to undergo crossbridge cycling with myosin, actin's affinity for tropomyosin, and the impact of actin acetylation on calcium regulated thin filament activation

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Oryctolagus Cuniculus (rabbit)

TISSUE(S): Skeletal Muscle

SUBMITTER: D. Brian Foster

LAB HEAD: Brian Foster

PROVIDER: PXD020732 | Pride | 2020-09-04

REPOSITORIES: pride

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			Action	DRS
	FileName_RO-CS-191017_CammaratoA_AC_Sample1.rawF027622.mzid.gz	Mzid
	FileName_RO-CS-191017_CammaratoA_AC_Sample1.rawF027622.mzid_File_Name__RO-CS-191017_CammaratoA_AC_Sample1.raw_F027622.MGF	Mzid
	FileName_RO-CS-191017_CammaratoA_AC_Sample1.rawF027623.mzid.gz	Mzid
	FileName_RO-CS-191017_CammaratoA_AC_Sample1.rawF027623.mzid_File_Name__RO-CS-191017_CammaratoA_AC_Sample1.raw_F027623.MGF	Mzid
	FileName_RO-CS-191017_CammaratoA_AC_Sample2.rawF027624.mzid.gz	Mzid

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