Table 2

Computationally determined sites of probable lipid binding. A matrix algorithm [11] was used to identify probable lipid-binding sites in the following cytoskeletal proteins; α-actinin [14], Arp2 [16], CapZβ-1 (submitted, TBMM), Talin [12-13, 121] and Vinculin [14]. In-vitro experimental support for the computationally predicted sites for α-Actinin, Arp2, Talin, and Vinculin (site 935–978) was obtained from a variety of techniques including hydrophobic labeling, differential scanning calorimetry (DSC), Langmuir Blodgett (film balance), T-jump, CD spectroscopy, cryo-electron microscopy (EM), FTIR, and isothermal titration calorimetry.
Protein	Sequence Residues	Species	Sequence	*Experimental (in-vitro) Validation*

α-actinin	281–300	Gallus gallus	EKLASDLLEWIRRTIPWLEN Residues (287–306) of 1HCI	DSC, Centrifugation, SDS-PAGE [14]
	720–739	Gallus gallus	QLLTTIARTINEVENQILTR Residues (726–745) of 1HCI	DSC, Centrifugation, SDS-PAGE [14]
Arp2	185–202	A. castellanii	RDVTRYLIKLLLLRGYVF	DSC, Film Balance, Temperature Jump [16]
CapZβ-1	134–151	Homo sapiens	IKKAGDGSKKIKGCWDSI	No data
	215–232	Homo sapiens	RLVEDMENKIRSTLNEIY	No data
Talin	385–406	M. musculatus	GEQIAQLIAGYIDIILKKKKSK	Isothermal Titration Calorimetry, Monolayer Expansion, CD-spectroscopy [15]; FTIR [86] Resonance energy transfer, Cryo-EM [90]
Vinculin	935–978	Gallus gallus	RLVRGGSGNKRALIQCAKDIAKASDEVT RLAKEVAKQCTDKRIR	Co-sedimentation, Hydrophobic Photolabeling [102]
	1020–1040	Gallus gallus	TEMLVHNAQNLMQSVKETVRE	No data
	1052–1066	Homo sapiens	AGFTLRWVRKTPWYQ	No data

Scott et al. Theoretical Biology and Medical Modelling 2006 3:17 doi:10.1186/1742-4682-3-17