ArticleProceedings of the National Academy of Sciences of the United States of America2000
Electrospray ionization mass spectrometry as a tool to analyze hydrogen/deuterium exchange kinetics of transmembrane peptides in lipid bilayers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 100 citations in OpenAlex.
- Probing protein-lipid interactions by hydrogen/deuterium exchange-mass spectrometry: advances, challenges and future directions.Chemical science · 2026Review
- Conformational Flexibility of Transmembrane Helices: How it Works and Where it Matters.Chemical reviews · 2026Review
- Hydrogen/deuterium exchange-mass spectrometry of integral membrane proteins in native-like environments: current scenario and the way forward.Essays in biochemistry · 2023Article
- The Archaeal NaFrontiers in chemistry · 2021Review
- Investigating the interactions of the first 17 amino acid residues of Huntingtin with lipid vesicles using mass spectrometry and molecular dynamics.Journal of mass spectrometry : JMS · 2020Article
- Ultrafast energy relaxation dynamics of amide I vibrations coupled with protein-bound water molecules.Nature communications · 2019Article
- Determination of Backbone Amide Hydrogen Exchange Rates of Cytochrome c Using Partially Scrambled Electron Transfer Dissociation Data.Journal of the American Society for Mass Spectrometry · 2018Article
- Dynamic distinctions in the NaThe Journal of biological chemistry · 2017Article
- Regio-Selective Intramolecular Hydrogen/Deuterium Exchange in Gas-Phase Electron Transfer Dissociation.Journal of the American Society for Mass Spectrometry · 2017Article
- The Influence of Lipid Bilayer Physicochemical Properties on Gramicidin A Conformer Preferences.Biophysical journal · 2016Article
- Asymmetric Preorganization of Inverted Pair Residues in the Sodium-Calcium Exchanger.Scientific reports · 2016Article
- Kinetics of peptide folding in lipid membranes.Biopolymers · 2015Review
- Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helix.Biophysical journal · 2014Article
- 2D IR cross peaks reveal hydrogen-deuterium exchange with single residue specificity.The journal of physical chemistry. B · 2013Article
- Evolution of the genetic code by incorporation of amino acids that improved or changed protein function.Journal of molecular evolution · 2013Article
- Integral membrane proteins and bilayer proteomics.Analytical chemistry · 2013Review
- The backbone dynamics of the amyloid precursor protein transmembrane helix provides a rationale for the sequential cleavage mechanism of γ-secretase.Journal of the American Chemical Society · 2013Article
- Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.International reviews in physical chemistry · 2013Article
- Mass spectrometry--from peripheral proteins to membrane motors.Journal of molecular biology · 2012Review
- Polar aprotic modifiers for chromatographic separation and back-exchange reduction for protein hydrogen/deuterium exchange monitored by Fourier transform ion cyclotron resonance mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
A method is described to study the precise positioning of transmembrane peptides in a phospholipid bilayer combining hydrogen/deuterium (H/D) exchange and nanoelectrospray ionization mass spectrometry. The method was tested by using model systems consisting of designed alpha-helical transmembrane peptides [acetylGW(2)(LA)(5)W(2)Aethanolamine (WALP16) and acetyl-(GA)(3)W(2)(LA)(5)W(2)(AG)(3)ethanolamine (WALP16(+10))] incorporated in large unilamellar vesicles of 1, 2-dimyristoyl-sn-glycero-3-phosphocholine. Both peptides consist of an alternating leucine/alanine hydrophobic core sequence flanked by tryptophan residues as interfacial anchor residues. In the case of WALP16(+10), this sequence is extended at both ends by 5-aa glycine/alanine tails extending into the aqueous phase surrounding the bilayer. H/D exchange of labile hydrogens in these peptides was monitored in time after dilution of the vesicles in buffered deuterium oxide. It was found that the peptides can be measured by direct introduction of the proteoliposome suspension into the mass spectrometer. Several distinct H/D exchange rates were observed (corresponding to half-life values varying from </=2 to approximately 2 x 10(4) min). Fast exchange rates were assigned to the water-exposed tails of WALP16(+10). For both WALP16 and WALP16(+10), intermediate exchange rates were assigned to the residues close to the membrane/water interface, and the slow exchange rates to the membrane-embedded hydrophobic core. These assignments were confirmed by results from collision-induced dissociation tandem mass spectrometry experiments, which allowed analysis of exchange of individual peptide amide linkages. This proteoliposome nanoelectrospray ionization mass spectrometry technique is shown to be an extremely sensitive and powerful tool for revealing site-specific information on peptide-membrane interactions.
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