TABLE 2.

Hydrophobic thickness (nm) of transmembrane peptides and proteins, and matching to lipid bilayers

	OPM*	Structure†	nP	dc (nm)
L16	–	2.7	17.5 ± 0.3	2.58 ± 0.05
L22	–	3.6	22.2 ± 1.2	3.47 ± 0.30
OmpF	2.42 ± 0.08	2.4	14.4 ± 0.3	2.00 ± 0.05
KcsA	3.31 ± 0.10	3.7	20.4 ± 0.5	3.13 ± 0.10
TbMscL	2.65 ± 0.38	1.8 or 3.4	16.2 ± 0.6	2.34 ± 0.11
EcMscL			15.8 ± 0.3	2.25 ± 0.06
SERCA	3.01 ± 0.18	2.1	20.7 ± 1.3	3.18 ± 0.24

n_P is the chain length of the diC(n_C:1)PtdCho with lowest free energy of association that is obtained by fitting with Eq. 14. d_c is the thickness of the hydrophobic core deduced from n_P by using Eq. 4.

^*Hydrophobic thickness deduced from thermodynamic principles, as listed in the OPM database (http://opm.phar.umich.edu/).

^†Hydrophobic thickness deduced from peptide or protein structure as given by Webb et al. (59) for peptides and by Lee (12) for proteins. Uncertainty for proteins is >±0.1 nm (A. G. Lee, University of Southampton, private communication, 2005).