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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

Ï„

PDB id

Δ G calc

D

Ï„

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).