Zobrazeno 1 - 9
of 9
pro vyhledávání: '"R.E. Koeppe nd"'
Publikováno v:
Biochemistry. 31:11283-11290
The orientation of the valine-1 side chain of gramicidin was determined by solid-state 2H NMR using valine-1-deuterated (d8) gramicidin. The peptide was incorporated into DMPC bilayers that were oriented between glass plates. When the plates were ori
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d0d68c5b58f16c11cdc753a865eb96c
https://doi.org/10.1021/bi00161a004
https://doi.org/10.1021/bi00161a004
Publikováno v:
Novartis Foundation Symposium 225-Gramicidin and Related Ion Channel-Forming Peptides
Mutations and chemical substitutions of amino acid side chains and backbone atoms have proved vital for understanding the folding, structure and function of gramicidin channels in phospholipid membranes. The channel's pore is lined by peptide backbon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ff04ad6c734bd6f7822197095ed8a101
https://doi.org/10.1002/9780470515716.ch4
https://doi.org/10.1002/9780470515716.ch4
Autor:
R.E. Koeppe nd, O S Anderson
Publikováno v:
Annual review of biophysics and biomolecular structure. 25
The chemical design or redesign of proteins with significant biological activity presents formidable challenges. Ion channels offer advantages for such design studies because one can examine the function of single molecular entities in real time. Gra
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82c5997e37fc693f1deca72d681ac7db
https://pubmed.ncbi.nlm.nih.gov/8800470
https://pubmed.ncbi.nlm.nih.gov/8800470
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
Publikováno v:
Biochemistry. 31(32)
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., &
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::320e4264575299d075b20e5ff3219461
https://pubmed.ncbi.nlm.nih.gov/1380823
https://pubmed.ncbi.nlm.nih.gov/1380823
Publikováno v:
Biophysical Journal. 61(3)
To the Editor: In several recent papers, NMR results for gramicidin A have been compared with predictions based on various models for a right-handed channel. In particular, 2H quadrupolar splittings (Hing et al., 1990a,b; Prosser et al., 1991) or '5N
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::834c30adac3ab55451b772b96ee28154
The structure of membrane-associated gramicidins can depend on the solvent in which they were dissolved prior to membrane incorporation (LoGrasso, P. V., F. Moll, and T. A. Cross 1988. Biophys. J. 54:259–267; Killian, J. A., K. U. Prasad, D. Hains,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e57f898c41d584751b10d803d5672c04
https://europepmc.org/articles/PMC1280745/
https://europepmc.org/articles/PMC1280745/
Publikováno v:
Biophysical Journal. 49(3):673-686
The modulation of gramicidin A single-channel characteristics by the amino acid side chains was investigated using gramicidin A analogues in which the NH2 terminal valine was chemically replaced by other amino acids. The replacements were chosen such
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9873717ec58ced6256c1eb38758bd5c3
Publikováno v:
Biophysical Journal. 45:263-276
The relation between chemical structure and permeability characteristics of transmembrane channels has been investigated with the linear gramicidins (A, B, and C), where the amino acid at position 1 was chemically replaced by phenylalanine, tryptopha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3820a11d93fdd99f523557371ca2d5f
https://doi.org/10.1016/s0006-3495(84)84153-3
https://doi.org/10.1016/s0006-3495(84)84153-3
Publikováno v:
Biophysical Journal. (3):527-533
Thermodynamic parameters for the binding of the monovalent cations, Li+, Na+, K+, Rb+, Cs+, NH4+, TI+, and Ag+, to gramicidin A and for the binding of TI+ to gramicidin C, incorporated into lysophosphatidylcholine, have been determined using a combin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd9983ccda42d9180ed813a6e09ce6e0