LEADER 04045nam 2200673Ia 450 001 9910144736703321 005 20170810191534.0 010 $a1-282-45526-5 010 $a9786612455261 010 $a0-470-51571-6 010 $a0-470-51572-4 035 $a(CKB)1000000000377224 035 $a(EBL)470768 035 $a(OCoLC)650074210 035 $a(SSID)ssj0000388273 035 $a(PQKBManifestationID)11272452 035 $a(PQKBTitleCode)TC0000388273 035 $a(PQKBWorkID)10411381 035 $a(PQKB)11324273 035 $a(MiAaPQ)EBC470768 035 $a(EXLCZ)991000000000377224 100 $a19990511d1999 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aGramicidin and related ion channel-forming peptides$b[electronic resource] /$f[editors, Derek J. Chadwick and Gail Cardew] 210 $aChichester ;$aNew York $cWiley$d1999 215 $a1 online resource (286 p.) 225 1 $aNovartis Foundation symposium ;$v225 300 $aDescription based upon print version of record. 311 $a0-471-98846-4 320 $aIncludes bibliographical references and indexes. 327 $aGRAMICIDIN AND RELATED ION PEPTIDES CHANNEL-FORMING; Contents; Participants; Introduction: gramicidin, a model ion channel; Correlations of structure, dynamics and function in the gramicidin channel by solid-state NMR spectroscopy; X-ray crystallographic structures of gramicidin and their relation to the Streptomyces Zividuns potassium channel structure; General discussion I; Design and characterization of gramicidin channels with side chain or backbone mutations; Engineering charge selectivity in alamethicin channels; Lorentzian noise in single gramicidin A channel forrnarnidiniurn currents 327 $aCan we use rate constants and state models to describe ion transport through gramicidin channels?The binding site of sodium in the gramicidin A channel; The mechanism of channel formation by alarnethicin as viewed by molecular dynamics simulations; General discussion I1; Ionic interactions in multiply occupied channels; Peptide influences on lipids; Peptide-lipid interactions and mechanisms of antimicrobial peptides; Folding patterns of membrane proteins: diversity and the limitations of their prediction 327 $aMolecular basis of the charge selectivity of nicotinic acetylcholine receptor and related ligand-gated ion channelsThe gramicidin-based biosensor: a functioning nano-machine; Final general discussion; Summary: what we have learned about gramicidin and other ion channels; Index of contributors; Subject Index 330 $aGramicidin channels have been studied intensively for more than 25 years. They serve as model transport systems for large protein ion channels, since it is difficult to glean high-resolution structural information on the latter. This book includes contributions from virtually all the major scientists studying gramicidin channels and is the only compilation of work in this field. It discusses crystallographic, spectroscopic, electrophysiological and computational studies, especially in the light of the recent availability of high-resolution structural data, and it compares these with insight 410 0$aNovartis Foundation symposium ;$v225. 606 $aGramicidins$vCongresses 606 $aIonophores$vCongresses 606 $aIon channels$vCongresses 608 $aElectronic books. 615 0$aGramicidins 615 0$aIonophores 615 0$aIon channels 676 $a572.65 676 $a572/.65 701 $aChadwick$b Derek$091632 701 $aCardew$b Gail$0857118 712 02$aNovartis Foundation. 712 12$aSymposium on Gramicidin and Related Ion Channel-forming Peptides$f(1998 :$eLondon, England) 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910144736703321 996 $aGramicidin and related ion channel-forming peptides$91920523 997 $aUNINA