Table 3
|
Characteristics of sequences implicated in lipid binding. The isolelectric point for the isolated peptide was calculated and the percent alpha-helix determined from the relevant crystal structure. The symbols for electrically positive residues are underlined ( |
||||||
| Protein |
Residues |
Sequence |
Number Residues |
Isoelectric Point |
Helix Content |
Sequence Site in Protein |
|
|
||||||
| α-actinin |
281–300 |
 |
20 |
4.49 |
15/20 (75%) |
Helices 1–2 |
| 720–739 |
 |
20 |
4.66 |
16/20 (80%) |
Carboxyl-terminal portion of Helix 16 |
|
| Arp2 |
185–202 |
 |
18 |
10.0 |
13/18 (72%) |
Helix 1 of Actin-like Subdomain 4 |
| CapZβ-1 |
134–151 |
 |
18 |
9.62 |
0/18 (0%) |
Contains portion of β strand 6 |
| 215–232 |
 |
18 |
4.49 |
18/18 (100%) |
Helix 5 |
|
| Talin |
385–406 |
 |
22 |
8.61 |
9/22 (41%) |
Helix 5 of Subdomain F3 of Talin-H |
| Vinculin |
935–978 |
 |
44 |
9.73 |
31/44 (70%) |
Domain 5, Helices 2–3 + amino-terminal portion of Helix 4 |
 |
||||||
| 1020–1040 |
 |
21 |
4.47 |
20/21 (95%) |
Domain 5, Helix 5 |
|
| 1052–1066 |
 |
15 |
Hairpin [122] |
|||
Scott et al. Theoretical Biology and Medical Modelling 2006 3:17 doi:10.1186/1742-4682-3-17 |
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); those corresponding to electrically negative residues are underlined (
). The characters under the amino acid sequence refer to the secondary structure; H = helix, T = hydrogen-bonded turn, S = bend, E = extended beta-strand, and B = residue in isolated beta-bridge. Residues 401–406 (KKKKSK) are not present in talin crystal structures. Helical residues are underlined (
).