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. 2005 Nov 4;90(2):470–479. doi: 10.1529/biophysj.105.068213

TABLE 2.

Non-natural peptides fitting the criteria indicated below

Peptide number Sequence Insertion angle (°) Mean hydrophobicity
22,319 U 5 U 9 4 O O 4 B 2 6 4 55 0.64
31,272 U B J 9 U 7 O U O J J 3 53 0.62
33,687 O O 2 Z 4 Z 3 O 6 5 9 X 26 0.66
48,482 O J 6 9 O 3 U 2 8 9 9 U 48 0.70
50,249 U 9 U 8 X 3 O 8 4 8 U 7 55 0.682
51,208 O U 7 8 Z X O 9 3 9 J U 35 0.67
52,230 O 3 8 O O B O 2 2 4 4 Z 52 0.69
56,571 U Z 6 J 8 5 X 7 U O X X 48 0.62
88,682 O 7 8 O 7 O 9 6 2 U Z 2 50 0.67
97,848 U 9 6 B O 9 O 6 X U 7 4 48 0.67
98,807 U O 8 7 6 O U 7 X J Z 9 53 0.68
99,721 U O 5 7 O 5 U 2 7 J 7 4 55 0.70

Mean hydrophobicity between 0.6 and 0.7, insertion angle between 35 and 55° and mass center located between 8 and 13 Å (absolute value) from the bilayer center in the IMPALA membrane, containing one ornithine or citrulline. The bold peptides are conformationally stable during angular dynamics. The boxed peptide was used in the experimental part of the study.