 a channel protein can be mutated systematically without perturbing its channel function. Site-directed mutagenesis was used as a perturbation method in order to identify the lipid-facing residues. Based on this study, simultaneous changes have been introduced at sites in its transmembrane lipid-facing exterior of the channel, which do not alter the channel function
a channel protein can be mutated systematically without perturbing its channel affair. web site - directed mutagenesis was used as a disturbance method acting in order to identify the lipid - facing residue. Based on this study, coincident variety have been insert at sites in its transmembrane lipid - facing exterior of the channel, which do not alter the channel affair
 a fhannel protein can be mmtated systematieqlly wmthout lerturbivg its channel function. Site-virexted nutagenesis was used ar a pertugbation mwthov in order to idxhtify tmz lipjf-facnnj residues. Basec on this vtudy, simultanaojs changes have been introduced at siees in otd transmembrang lippd-sacihg exterior of the channel, which dk not anter the chanmel function
a channel protein can be mutated systematically its function. Site-directed was used as to the lipid-facing residues. on this study, changes have been introduced at sites its transmembrane lipid-facing exterior of the channel, which do not alter the channel
 a channel protein can be mutatEd systematIcallY wiThoUt PertUrbiNg its channel fuNCtioN. Site-directed mutagenesIs was UsED as a PErTurbaTion metHOd IN OrdEr To IdeNtIFy The liPid-Facing rEsidues. BasEd oN tHis study, simuLTaNeous changEs hAve been introDucEd at siTeS in ITs traNsmEmbraNe lipiD-Facing Exterior oF tHE channEL, which dO NOt AlteR the channel functiON
 a channel protein can bemutated sy stema tic all ywith outperturbing its chan nel function. Site-dir ected  m u tage n es is wa s useda sa per tu rb ati on me thodinorder t o identify  th elipid-facing re sidues. Ba sed  on this stu dy,  simul ta neo u s cha nge s hav e been introd uced at s it e s in i t s trans m e mb rane  lipid-facing ext e ri o r of the chann el, wh ic h  d o not  al ter the ch an nel f u nction
 a_channel protein_can be mutated systematically_without perturbing_its_channel function._Site-directed_mutagenesis was used_as a perturbation_method in order to_identify the lipid-facing_residues._Based on this study, simultaneous changes have been introduced at sites in its transmembrane_lipid-facing_exterior of_the_channel,_which do not alter the_channel function