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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.

From: Protein-lipid interactions: correlation of a predictive algorithm for lipid-binding sites with three-dimensional structural data

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