CONFORMATION AND ENVIRONMENT OF CHANNEL FORMING PEPTIDES: A SIMULATION STUDY. Export

@article{citeulike:500587, abstract = {Ion channel forming peptides enable us to study the conformational dynamics of a transmembrane helix as a function of sequence and environment. Molecular dynamics simulations are used to study the conformation and dynamics of three 22-residue peptides derived from the second transmembrane domain of the glycine receptor (NK4-M2GlyR-p22). Simulations are performed on the peptide in four different environments: trifluoroethanol/water; SDS micelles; DPC micelles; and a DMPC bilayer. A hierarchy of \'{a}-helix stabilisation between the different environments is observed such that TFE/water < micelles < bilayers. Local clustering of trifluoroethanol molecules around the peptide appears to help stabilise an \'{a}-helical conformation. Single (S22W) and double (S22W,T19R) substitutions at the C-terminus of NK4-M2GlyR-p22 help to stabilise a helical conformation in the micelle and bilayer environments. This correlates with the ability of the W22 and R19 sidechains to form H-bonds with the headgroups of lipid or detergent molecules. This study provides a first atomic resolution comparison of the structure and dynamics of NK4-M2GlyR-p22 peptides in membrane and membrane-mimetic environments, paralleling NMR and functional studies of these peptides.}, address = {University of Oxford.}, author = {Johnston, Jennifer and Cook, Gabriel and Tomich, John and Sansom, Mark S S.}, citeulike-article-id = {500587}, citeulike-linkout-0 = {http://dx.doi.org/10.1529/biophysj.105.069625}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/16387778}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=16387778}, day = {30}, doi = {10.1529/biophysj.105.069625}, issn = {0006-3495}, journal = {Biophys J}, keywords = {biology, lipids, molecular, simulation}, month = {December}, posted-at = {2006-10-31 15:47:25}, priority = {2}, title = {CONFORMATION AND ENVIRONMENT OF CHANNEL FORMING PEPTIDES: A SIMULATION STUDY.}, url = {http://dx.doi.org/10.1529/biophysj.105.069625}, year = {2005} }

TY - JOUR ID - citeulike:500587 L3 - citeulike-article-id:500587 N2 - Ion channel forming peptides enable us to study the conformational dynamics of a transmembrane helix as a function of sequence and environment. Molecular dynamics simulations are used to study the conformation and dynamics of three 22-residue peptides derived from the second transmembrane domain of the glycine receptor (NK4-M2GlyR-p22). Simulations are performed on the peptide in four different environments: trifluoroethanol/water; SDS micelles; DPC micelles; and a DMPC bilayer. A hierarchy of á-helix stabilisation between the different environments is observed such that TFE/water < micelles < bilayers. Local clustering of trifluoroethanol molecules around the peptide appears to help stabilise an á-helical conformation. Single (S22W) and double (S22W,T19R) substitutions at the C-terminus of NK4-M2GlyR-p22 help to stabilise a helical conformation in the micelle and bilayer environments. This correlates with the ability of the W22 and R19 sidechains to form H-bonds with the headgroups of lipid or detergent molecules. This study provides a first atomic resolution comparison of the structure and dynamics of NK4-M2GlyR-p22 peptides in membrane and membrane-mimetic environments, paralleling NMR and functional studies of these peptides. JF - Biophys J SN - 0006-3495 AD - University of Oxford. TI - CONFORMATION AND ENVIRONMENT OF CHANNEL FORMING PEPTIDES: A SIMULATION STUDY. KW - biology KW - lipids KW - molecular KW - simulation AU - Johnston, Jennifer AU - Cook, Gabriel AU - Tomich, John AU - Sansom, Mark S PY - 2005/12/30/ UR - http://dx.doi.org/10.1529/biophysj.105.069625 ER -