| 1spf » Pulmonary surfactant-associated protein C | |
|---|---|
| Hydrophobic Thickness | 31.7 ± 3.3 Å |
| Tilt Angle | 21 ± 0° |
| ΔGtransfer | -32.0 kcal/mol |
| Links to 1spf | PDB Sum, PDB, SCOP, MSD, OCA, MMDB |
| Topology | subunit A (N-terminus in) |
| Resolution | NMR |
| Other PDB entries of this protein | 2esy |
| Number of TM Secondary Structures | 1 |
| Experimental Verification for 1spf » Pulmonary surfactant-associated protein C |
|---|
| This peptide forms a hydrophopbic alpha-helix, with a transmembrane orientation (Vandenbussche et al. 1992). |
| 1 reference |
|---|
| Vandenbussche G, Clercx A, Curstedt T, Johansson J, Jornvall H, Ruysschaert JM. 1992. Structure and orientation of the surfactant-associated protein C in a lipid bilayer. Eur J Biochem. 203:201-9. PubMed |
| Comments on 1spf » Pulmonary surfactant-associated protein C |
|---|
| Pulmonary surfactant associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. This is full-length peptide. |