Molecular and channel-forming characteristics of gramicidin K's: a family of naturally occurring acylated gramicidins
| Autor: | L.P. Williams, M J Taylor, R.E. Koeppe nd, James F. Hinton, G R Waller, Olaf S. Andersen, E J Narcessian, J P Lazenby |
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| Rok vydání: | 1992 |
| Předmět: |
Magnetic Resonance Spectroscopy
Stereochemistry Protein Conformation Acylation Molecular Sequence Data Biochemistry Models Biological Ion Channels Mass Spectrometry chemistry.chemical_compound Protein structure Gramicidin K Ethanolamine polycyclic compounds medicine Amino Acid Sequence Gramicidin B Peptide sequence chemistry.chemical_classification technology industry and agriculture Electric Conductivity Gramicidin Fatty acid Kinetics medicine.anatomical_structure chemistry Membrane protein Thermodynamics lipids (amino acids peptides and proteins) |
| Zdroj: | Biochemistry. 31(32) |
| ISSN: | 0006-2960 |
| Popis: | The gramicidin K family is a set of naturally occurring acylated linear peptides in which a fatty acid is esterified to the ethanolamine hydroxyl of either gramicidin A or C, and possibly also to gramicidin B (Koeppe, R. E., II, Paczkowski, J. A., & Whaley, W. L. (1985) Biochemistry 24, 2822-2826). These acylated gramicidins form membrane-spanning channels in planar lipid bilayers and therefore constitute a model system with which to study the structural and functional consequences of acylation on membrane proteins. This paper serves to characterize further the channels formed by acylated gramicidins A and C and to demonstrate that these channels are structurally equivalent to the channels formed by the standard gramicidins. We also present additional evidence for the ester linkage in the natural acylated gramicidins A and C and identify the fatty acyl chains. |
| Databáze: | OpenAIRE |
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