By Novartis Foundation, Novartis Foundation Symposium
Gramicidin channels were studied intensively for greater than 25 years. They serve as version delivery platforms for giant protein ion channels, because it is hard to glean high-resolution structural info at the latter.
This booklet comprises contributions from nearly all of the major scientists learning gramicidin channels and is the one compilation of labor during this box. It discusses crystallographic, spectroscopic, electrophysiological and computational reviews, in particular within the gentle of the hot availability of high-resolution structural info, and it compares those with insights derived from better platforms. in addition to drawing jointly a lot new and intriguing paintings during this box, it offers tips to promising new learn instructions.
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Additional info for Novartis Foundation Symposium 225 - Gramicidin and Related Ion Channel-Forming Peptides
1A) and methanol (Fig. 1B) have recently been re-refined (Burkhart et a1 1997). Both are at high resolution and differ in mostly minor ways from the structures originally GRAMICIDIN CRYSTAL STRUCTURES 25 reported in these solvents (Langs 1988, Langs et a1 1991). 06 A2 for all atoms. The major differences appear to be that different side chains are assigned to have multiple positions in the original and rerefined structures. 16) upon re-refinement. The structure of an uncomplexed form prepared from n-propanol (Fig.
Cigar-like structures), possibly two-dimensional crystals. In all cases examined, the crystals that grew didn’t have the same final 1ipid:gramicidin ratio that was in the initial crystallization mixture. However, if we tried to set up the crystals with the final 1ipid:gramicidin ratio, we didn’t get any crystals growing at all. Killiun: Have you tried using glycolipids? Because there may be a specific interaction between the tryptophan side chains and the glycosyl moiety. Wulluce: No, but it’s a good suggestion.
We found, to our amazement, that the same fixed charge for the channel fits all of the data. One extra constant per ion, namely a diffusion coefficient, and one charge are sufficient to fit all of the data. e. the charge of the protein, is involved. Smart: Is it possible to resolve the difference between the Cross and Roux views of the ion-binding position by performing a back calculation of what NMR observables could be expected to be measured based on the molecular dynamics trajectories Roux has performed?