Conformational changes of surfactant protein B due to the alveolar air/liquid interface using molecular dynamics.

ABSTRACT:

Context

Surfactant protein B (SP-B) is a critically important component of pulmonary surfactant (PS), responsible for much of the lipid restructuring activity necessary to maintain proper respiratory function. Despite its functional and biological importance, there is a significant lack of knowledge regarding the structural characteristics of SP-B, exacerbated by a lack of a complete, experimentally determined structure. Comparative modeling with homologous saposin-family proteins was used to generate predicted structures for SP-B in both an open (hydrophobic residues exposed) and closed (hydrophobic residues buried) conformation. These structures were then used for further study with molecular dynamics. Five replicate simulation systems were prepared for both conformations in diff

SUBMITTER: Locke T 

PROVIDER: S-EPMC12678512 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature