Structure and influence on stability and activity of the N-terminal propetide part of lung surfactant protein C
Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C
peptide synthesis using f-Moc chemistry. The sequence of the peptide is naturally found in Human.
structures with favorable non-bond energy,structures with the least restraint violations,structures with the lowest energy,target function
the structures are based on a total of 344 restraints, 263 are NOE-derived distance constraints, 81 dihedral angle restraints
closest to the average,fewest violations,lowest energy
0.5mM SP-Ci(1-31) in 35mM [2H38]dodecylphosphocholine (DPC), 50mM sodium phosphate buffer
N-terminal part of lung surfactant protein C, LIPID BINDING PROTEIN