Table 1.
P. no. | Peptide seq | Oriental of protein in membrane | Membrane-embedded amino acid residues (in hydrocarbon core) | |||
---|---|---|---|---|---|---|
Depth/hydrophobic thickness (Å) | Gtransfer (kcal/mol) | Tilt angle | Tilt | Embedded residues | ||
1 | MDEFIERYKLEGY | 4.5 ± 1.7 | − 5.1 | 78.0 ± 18.0° | 78 | 1, 4–5, 8 |
2 | PYEDFQENWNTKH | 3.4 ± 2.1 | − 4.1 | 80.0 ± 15.0° | 80 | 5, 9, 13 |
3 | LQDVVNQNAQALN | 1.7 ± 1.6 | − 3.1 | 52.0 ± 11.0° | 52 | 1, 4 |
4 | YDYCIPYNSVTSS | 2.3 ± 0.4 | − 4.6 | 88.0 ± 7.0° | 88 | 1, 5–7 |
5 | YVYSRVKNLNSSR | 2.6 ± 1.6 | − 4.5 | 75.0 ± 8.0° | 75 | 2–3, 6 |
6 | NGTITVEELKKLL | 3.6 ± 0.8 | − 7.9 | 85.0 ± 7.0° | 85 | 1, 4, 6, 9, 12–13 |
7 | TENKYSQLDEEQP | 2.2 ± 1.1 | − 3.4 | 79.0 ± 13.0° | 79 | 4, 8 |
8 | SPKLFIRQEEVQE | 2.2 ± 1.8 | − 2.1 | 86.0 ± 13.0° | 86 | 8 |
9 | FSLELQDHNETCH | 1.6 ± 1.7 | − 3.6 | 72.0 ± 17.0° | 72 | 1–3, 5 |
10 | FYEDFLEYHDVRV | 2.6 ± 12.5 | − 3.9 | 79.0 ± 14.0° | 79 | 6,8,13 |
11 | DQELIRQGTDYKH | 2.0 ± 1.1 | − 2.8 | 76.0 ± 10.0° | 76 | 5 |
12 | SRNYIAQVDVVNF | 2.7 ± 1.6 | − 5.1 | 85.0 ± 11.0° | 85 | 4–8, 12–13 |
This table displays transmembrane of lipid-interacted embedded amino acid residues in single line with each highlighted in bold, while the rest of the residues in italic