Accession Number : ADA188740
Title : Studies of Model Ion Channels in Defect-Free Multibilayers of Phospholipids.
Descriptive Note : Annual rept. Oct 86-Sep 87,
Corporate Author : RICE UNIV HOUSTON TEX DEPT OF PHYSICS
Personal Author(s) : Huang, Heuy W
PDF Url : ADA188740
Report Date : 15 Nov 1987
Pagination or Media Count : 4
Abstract : Model ion channels such as gramicidin, melittin and alamethicin exhibit functional similarities to physiological channels, including voltage-gating, selectivities, activation and inactivation. Since the structural studies of physiological channels are extremely difficult, the structure-function relations revealed in model channels may provide valuable insights into the physical basis of biological sensory. A great deal of functional (electrical) properties of model channels is known, but with the exception of gramicidin (which is not a voltage-gated channel) little progress has been made in determining the structures of the channels in membrane. We have developed a technique of preparing defect-free lipid multibilayers with ion channels embedded in them, so that spectroscopic and scattering measurements of aligned ion channels in electric field can be made. CD studies of alamethicin channels showed the important orientation effect of -helical peptides on CD and conformation changes of the channel with sample conditions.
Descriptors : *PEPTIDES, *PHOSPHOLIPIDS, *IONIC CURRENT, *ELECTROPHYSIOLOGY, *MEMBRANES(BIOLOGY), ACTIVATION, CHANNELS, ELECTRIC FIELDS, HELIXES, IONS, MEASUREMENT, MODELS, ORIENTATION(DIRECTION), PHYSIOLOGY, SCATTERING, SPECTROSCOPY, MOLECULAR STRUCTURE, AMINO ACIDS, LAYERS
Subject Categories : Biochemistry
Anatomy and Physiology
Distribution Statement : APPROVED FOR PUBLIC RELEASE