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Table 6 Calculated parameters of open and closed states of membrane-associated proteins: binding energies (ΔG calc , kcal/mol), penetration depths (D, Å), and tilt angles (τ, °).

From: The role of hydrophobic interactions in positioning of peripheral proteins in membranes

Protein Category "Closed" state "Open"/lipid-bound state
   PDB id Δ G calc D τ PDB id Δ G calc D τ
Cytochrome P450 2b4 A.1 1suo -13.0 4.7 54 2bdm -18.2 10.5 45
Fungal lipase 1 C.1 1trh -7.8 3.0 80 1lpp -30.6 9.1 84
Triacylglycerol lipase Rhizomucor miehei C.1 3tgl -4.1 4.5 28 4tgl -14.0 4.9 55
Triacylglycerol lipase Humicola lanuginose C.1 1tib -3.3 1.9 42 1ein -13.5 9.5 71
Gastric lipasea C.1 1hlg -5.0 3.4 6 1k8q -10.8 6.3 80
α-Toxin (Phospholipase C) C.1 1gyg -4.2 5.5 60 1ca1 -4.5 2.2 88
Alpha-tocopherol transfer protein C.2 1r5l -10.6 4.0 81 1oiz -20.7 8.4 63
Glycolipid transfer protein C.2 1swx -4.9 3.4 86 1sx6 -7.9 3.9 87
Ganglioside GM2 activator C.2 2ag4 -5.1 4.2 47 1tjj -9.3 4.6 55
Synaptotagmin C2A domain of b C.4 1rsy -3.3 2.1 26 1bync -4.4 3.7 36
Mersacidind C.7 1mqxc -2.3 2.4 77 1mqyc -9.5 11.5 56
  1. a The open and closed forms of gastric lipase are taken from closely related species.
  2. b Ca2+-free structure (1rsy) versus Ca2+-bound structure (1byn). Ca2+ -bound state is usually referred as associated with the lipid bilayer.
  3. c Structures determined by solution NMR spectroscopy. All other structures were solved by X-ray crystallography.
  4. d "Closed" – structure in methanol solution, "open" – structure in DPC micelles. Crystal structure of the peptide (1qow) has intermediate values of ΔG calc = -7.9 kcal/mol and D = 6.9A (in the monomeric state).
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