Structure at 2.5 A of a designed peptide that maintains solubility of membrane proteins.
A 24-amino acid peptide designed to solubilize integral membrane proteins has been synthesized. The design was for an amphipathic alpha helix with a "flat" hydrophobic surface that would interact with a transmembrane protein as a detergent. When mixed with peptide, 85 percent of bacteriorhodopsin and 60 percent of rhodopsin remained in solution over a period of 2 days in their native forms. The crystal structure of peptide alone showed it to form an antiparallel four-helix bundle in which monomers interact, flat surface to flat surface, as predicted.
Schafmeister
C E
CE
Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.
Miercke
L J
LJ
Stroud
R M
RM
D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000737:chemistry; D018360:Crystallography, X-Ray; D003902:Detergents / Q000138:chemical synthesis / Q000737:chemistry*; D015195:Drug Design; D008565:Membrane Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012243:Rhodopsin / Q000737:chemistry
D003902:Detergents; D008565:Membrane Proteins; D010455:Peptides; C083798:peptitergent PD1; D001436:Bacteriorhodopsins; D012243:Rhodopsin