Studies on the insolubility of a transmembrane peptide from signal peptide peptidase.
We have undertaken fundamental studies on the solubility properties of a peptide derived from the fourth transmembrane (TM) domain of signal peptide peptidase, a 7-TM intramembrane-cleaving protease. We have found that by disfavoring secondary structure formation we are able to greatly improve the solubility, handling, and purification properties of this peptide. Our findings suggest that preventing secondary structure formation by reversible modification of the polypeptide backbone of hydrophobic transmembrane peptides may be a useful strategy for the total chemical protein synthesis of integral membrane proteins.
Johnson
Erik C B
EC
Institute for Biophysical Dynamics, Department of Biochemistry and Molecular Biology, The University of Chicago, 920 East 58th Street, Chicago, Illinois 60637, USA.
Kent
Stephen B H
SB
D016282:Aspartic Acid Endopeptidases / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D008565:Membrane Proteins / Q000138:chemical synthesis* / Q000737:chemistry; D008958:Models, Molecular; D011487:Protein Conformation; D012995:Solubility
D008565:Membrane Proteins; D016282:Aspartic Acid Endopeptidases; C460085:signal peptide peptidase