Abstract
MscL, a large-conductance mechanosensitive (MS) ion channel, functions as a fast osmolyte release valve to reduce hydrostatic pressure within the cytoplasmic membrane upon osmotic shock. These membrane proteins play a crucial role in fundamental biological processes, including but not limited to blood and osmotic pressure regulation, touch and pain-sensing, and cardiovascular control. In this work, we study the effects of disrupting the ‘hydrophobic lock’ in M. tuberculosis wild-type MscL through mutations (V21T, V21A, V21T, and A20N) at the interface of transmembrane helix 2 that lines the pore.
Sign-in/Register to access full text options 
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 callDisclaimer: 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.
