. Author manuscript; available in PMC: 2012 Nov 25.

Published in final edited form as: J Mol Biol. 2011 Oct 1;414(2):204–216. doi: 10.1016/j.jmb.2011.09.035

Table 3.

Summary of potential contact areas between actin and myosin

Type of interaction		Actin	^aMyosin

	Peptide	Residues probed in this study	Peptides from Cryo-EM models
Ionic	D1-K18	L8, C10, L16, K18	Y626-Q647^A,^B,^C,^D
Ionic	A19-R28	F21	Y626-Q647^A,^B,^C,^D

Hydrophobic and ionic	A29-R39	P32, P38	N552-H558^A,^B

Potential hydrogen bonding	G46-K50	C46, C47, C48, C49, C50	S549-H558^C^(partial),^D

Ionic	I85-R95	W86, H87, H88, F90, Y91, R95	K567-H578^A,^B,^C,^D
Ionic	V96-K113	E99, E100, H101, P102, P112/K113	K567-H578^A,^B,^C,^D

Hydrophobic and ionic	M119-R117	M119, M123, F124, Y143	P529-K553^A,^B,^C,^D& Y403-G416 (for 336-359 peptide)^A,^B,^C,^D
	T148-R177	H161, Y166, Y169, L171, P172, H173, M176
	R336-K359	Y337, L346, L349, F352, M355

Actin residues are those probed in the present study.

Myosin segments proposed to bind actin in the previous electron microscopy based models of acto-S1 (

Rayment et al., 1993,

Milligan, 1996,

Volkman et al., 2000, and

Lorenz and Holmes, 2010.).