ArticleBiophysical journal2006
Tryptophan contributions to the empirical free-energy profile in gramicidin A/M heterodimer channels.
Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- The membrane interface dictates different anchor roles for "inner pair" and "outer pair" tryptophan indole rings in gramicidin A channels.Biochemistry · 2011Article
- Gramicidin channels are internally gated.Biophysical journal · 2010Article
- The gramicidin channel ion permeation free-energy profile: direct and indirect effects of CHARMM force field improvements.Interdisciplinary sciences, computational life sciences · 2009Article
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Authors and funding
3 authors.
Funding
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Abstract
Gramicidin A/gramicidin M heterodimer conductances were measured in planar lipid bilayers and found to form two distinguishable populations about halfway between the gramicidin A and gramicidin M homodimer conductances. This implies that the principle difference in the gramicidin A and gramicidin M transport free-energy profiles occurs at the channel center, where it would produce similar effects on the rate-limiting barrier for the two heterodimers. Kinetic analysis based on this and nearly all previously published homodimer conductance data for both gramicidin A and gramicidin M channels confirms this conclusion, indicating that the translocation step is approximately 100-fold slower in gramicidin M homodimers than in gramicidin A homodimers and that first- and second-ion exit-rate constants are higher by factors of 24 and 10, respectively. Assuming that the ratios of rate constants are related to the free-energy difference between gramicidin A and gramicidin M, we construct an effective ion-Trp free-energy interaction profile that has a minimum at the channel center.
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