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• W2040570168 endingPage "428" @default.
• W2040570168 startingPage "419" @default.
• W2040570168 abstract "The linear ion channel peptide gramicidin represents an excellent model for exploring the principles underlying membrane protein structure and function, especially with respect to tryptophan residues. The tryptophan residues in gramicidin channels are crucial for the structure and function of the channel. In order to test the importance of indole hydrogen bonding for the biophysical properties of gramicidin channels, we monitored the effect of N-methylation of gramicidin tryptophans, using a combination of steady state and time-resolved fluorescence approaches along with circular dichroism spectroscopy. We show here that in the absence of the hydrogen bonding ability of tryptophans, tetramethyltryptophan gramicidin (TM-gramicidin) is unable to maintain the single stranded, head-to-head dimeric channel conformation in membranes. Our results show that TM-gramicidin displays a red-shifted fluorescence emission maximum, lower red edge excitation shift (REES), and higher fluorescence intensity and lifetime, consistent with its nonchannel conformation. This is in agreement with the measured location (average depth) of the 1-methyltryptophans in TM-gramicidin using the parallax method. These results bring out the usefulness of 1-methyltryptophan as a fluorescent tool to examine the hydrogen bonding ability of tryptophans in proteins and peptides. We conclude that changes in the hydrogen bonding ability of tryptophans, along with coupled changes in peptide backbone structure induce the loss of single stranded β(6.3) helical dimer conformation. These results agree with earlier results from size-exclusion chromatography and single-channel measurements for TM-gramicidin, and confirm the importance of indole hydrogen bonding for the conformation and function of ion channels and membrane proteins." @default.
• W2040570168 created "2016-06-24" @default.
• W2040570168 creator A5023572938 @default.
• W2040570168 creator A5044485493 @default.
• W2040570168 creator A5060301743 @default.
• W2040570168 creator A5063835467 @default.
• W2040570168 creator A5076949358 @default.
• W2040570168 date "2014-01-01" @default.
• W2040570168 modified "2023-10-17" @default.
• W2040570168 title "Importance of indole NH hydrogen bonding in the organization and dynamics of gramicidin channels" @default.
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• W2040570168 doi "https://doi.org/10.1016/j.bbamem.2013.10.011" @default.
• W2040570168 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3975908" @default.
• W2040570168 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24148157" @default.
• W2040570168 hasPublicationYear "2014" @default.
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