ArticleThe journal of physical chemistry letters2012
Environment Polarity in Proteins Mapped Noninvasively by FTIR Spectroscopy.
Article in The journal of physical chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Nanoparticle classification, physicochemical properties, characterization, and applications: a comprehensive review for biologists.Journal of nanobiotechnology · 2022Review
- Conformation-specific detection of calmodulin binding using the unnatural amino acid p-azido-phenylalanine (AzF) as an IR-sensor.Structural dynamics (Melville, N.Y.) · 2018Article
- Infrared and fluorescence assessment of the hydration status of the tryptophan gate in the influenza A M2 proton channel.Physical chemistry chemical physics : PCCP · 2016Article
- Probing Site-Specific Structural Information of Peptides at Model Membrane Interface In Situ.Journal of the American Chemical Society · 2015Article
- Strength of a bifurcated H bond.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Two-dimensional sum-frequency generation reveals structure and dynamics of a surface-bound peptide.Journal of the American Chemical Society · 2014Article
- Calculations of the electric fields in liquid solutions.The journal of physical chemistry. B · 2013Article
- Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamage.Biochemistry · 2013Article
- Quantification of transition dipole strengths using 1D and 2D spectroscopy for the identification of molecular structures via exciton delocalization: application to α-helices.The Journal of chemical physics · 2012Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The polarity pattern of a macromolecule is of utmost importance to its structure and function. For example, one of the main driving forces for protein folding is the burial of hydrophobic residues. Yet polarity remains a difficult property to measure experimentally, due in part to its non-uniformity in the protein interior. Herein, we show that FTIR linewidth analysis of noninvasive 1-(13)C=(18)O labels can be used to obtain a reliable measure of the local polarity, even in a highly multi-phasic system, such as a membrane protein. We show that in the Influenza M2 H(+) channel, residues that line the pore are located in an environment that is as polar as fully solvated residues, while residues that face the lipid acyl chains are located in an apolar environment. Taken together, FTIR linewidth analysis is a powerful, yet chemically non-perturbing approach to examine one of the most important properties in proteins - polarity.
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.