Conformational study of signal peptides of the LamB protein.
A molecular mechanics study of a portion of the signal peptide of LamB protein, a mutant and two revertants, has been carried out. The peptides studied are: (I) Leu-Pro-Leu-Ala-Val-Ala-Val-Ala-Ala-Gly-Val for the wild type signal peptide; a mutant which shows no export capability (II), Leu-Pro-Val-Ala-Ala-Gly-Val; and two revertants with replacements of Pro by Leu (III), and Gly by Cys (IV) respectively. The results found are in agreement with the experimental data available; the aim of this work being to provide evidence of conformational features necessary along the export mechanisms. The present study suggests that both an alpha helix formation capability and a certain hydrophobicity of the peptide chain are the characteristics required for export competence.
Perez
J J
JJ
Dpt. d'Enginyeria Quimica, UPC, Barcelona, Spain.
Ricart
J M
JM
Masip
J
J
D000595:Amino Acid Sequence; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018272:Porins; D011487:Protein Conformation; D021382:Protein Sorting Signals / Q000737:chemistry*; D011991:Receptors, Virus / Q000737:chemistry* / Q000235:genetics; D013816:Thermodynamics
D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D021382:Protein Sorting Signals; D011991:Receptors, Virus; C016532:maltoporins