Abstract

Circular dichroism experiments show that a 28 residue transmembrane peptide derived from the R. sphaeroides bacterial flagellar motor protein MotB adopts predominantly β-sheet conformation when bound within phosphatidylcholine vesicles. A peptide with a mutation at Asp32, which has been shown to destroy proton conductance, is also shown to insert into the model membrane in predominantly β-sheet conformation, suggesting that it is not the gross structural features of the transmembrane region that are disrupted by this mutation but perhaps only the electrostatic properties of the pore. A tentative structure for a MotB pore is proposed which consists of an eight stranded β-barrel.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.