Hydrogen Bond Arrangement Is Shown to Differ in Coexisting Phases of Aqueous Two-Phase Systems

Madeira, Pedro P.; Titus, Amber R.; Ferreira, Luísa A.; Belgovskiy, Alexander I.; Mann, Elizabeth K.; Mann, J. Adin; Meyer, William V.; Smart, Anthony E.; Uversky, Vladimir N.; Zaslavsky, Boris Y.

doi:10.3390/biom11121787

Cited by 7 publications

(15 citation statements)

References 37 publications

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respectively. The fit includes the four Gaussian expressions identified by the subscript, with baseline B and normalization by A to the measured total amplitude, where

is the standard deviation of each Gaussian component, and

is the amplitude contribution of each:

…”

Section: Methodssupporting

confidence: 91%

“…This method may not therefore be used for many proteins such as serum albumin or lysozyme. We recently used ATR-FTIR spectroscopy to show that the solvent features of water are strongly correlated with hydrogen bond arrangement in solutions of various compounds [ 17 , 18 , 19 , 20 , 21 , 22 ]; here we use it to explore the rearrangement of hydrogen bonds in aqueous solutions of several globular proteins.…”

Section: Introductionmentioning

confidence: 99%

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Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins

Titus

Madeira²,

Ferreira

et al. 2022

IJMS

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This work presents the first evidence that dissolved globular proteins change the arrangement of hydrogen bonds in water, with different proteins showing quantitatively different effects. Using ATR-FTIR (attenuated total reflection—Fourier transform infrared) spectroscopic analysis of OH-stretch bands, we obtain quantitative estimates of the relative amounts of the previously reported four subpopulations of water structures coexisting in a variety of aqueous solutions. Where solvatochromic dyes can measure the properties of solutions of non-ionic polymers, the results correlate well with ATR-FTIR measurements. In protein solutions to which solvatochromic dye probes cannot be applied, NMR (nuclear magnetic resonance) spectroscopy was used for the first time to estimate the hydrogen bond donor acidity of water. We found strong correlations between the solvent acidity and arrangement of hydrogen bonds in aqueous solutions for several globular proteins. Even quite similar proteins are found to change water properties in dramatically different ways.

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respectively. The fit includes the four Gaussian expressions identified by the subscript, with baseline B and normalization by A to the measured total amplitude, where

is the standard deviation of each Gaussian component, and

is the amplitude contribution of each:

…”

Section: Methodssupporting

confidence: 91%

Section: Introductionmentioning

confidence: 99%

Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins

Titus

Madeira²,

Ferreira

et al. 2022

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…We found that the best and most reliable fits gave peak frequencies within the error band of values from literature [22], which were therefore fixed for all later fitting routines. These values, which we confirmed earlier [17,20], are 3080 cm -1 , 3230 cm -1 , 3400 cm -1 , and 3550 cm -1 , represented by 𝜇𝜇 1−4 respectively. The fit includes the four Gaussian expressions identified by the subscript, with baseline B and normalization by A to the measured total amplitude, where 𝜎𝜎 𝑖𝑖 is the standard deviation of each Gaussian component, and 𝑎𝑎 𝑖𝑖 is the amplitude contribution of each:…”

Section: Analysis Of Atr-ftir Spectrasupporting

confidence: 89%

“…Previously reported solvent properties of water [20], such as solvent dipolarity/polarizability, π*, solvent H-bond donor acidity, α, and solvent H-bond acceptor basicity, β, correlate strongly with the fractional contributions of subpopulations of water. This approach was used successfully to analyze the coexisting phases of several aqueous two-phase systems [17]. We apply the same model here for the analysis of water in solutions of different globular proteins.…”

Section: Analysis Of Atr-ftir Spectramentioning

confidence: 99%

“…This method may not therefore be used for many proteins such as serum albumin or lysozyme. We recently used ATR-FTIR spectroscopy to show that the solvent features of water are strongly correlated with hydrogen bond arrangement in solutions of various compounds [17][18][19][20][21][22]; here we use it to explore the rearrangement of hydrogen bonds in aqueous solutions of several globular proteins.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins

Titus¹,

Madeira²,

Ferreira³

et al. 2022

Preprint

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This work presents the first evidence that dissolved globular proteins change the arrangement of hydrogen bonds in water, with different proteins showing quantitatively different effects. Using ATR-FTIR (Attenuated Total Reflection – Fourier Transform Infrared) spectroscopic analysis of OH-stretch bands, we obtain quantitative estimates of the relative amounts of the previously reported four subpopulations of water structures coexisting in a variety of aqueous solutions. Where solvatochromic dyes can measure the properties of solutions of non-ionic polymers, the results correlate well with ATR-FTIR measurements. In protein solutions to which solvatochromic dye probes cannot be applied, NMR (Nuclear Magnetic Resonance) spectroscopy was used for the first time to estimate the hydrogen bond donor acidity of water. We found strong correlations between the solvent acidity and arrangement of hydrogen bonds in aqueous solutions for several globular proteins. Even quite similar proteins are found to change water properties in dramatically different ways.

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Membraneless Compartmentalization of Cell‐Free Transcription‐Translation by Polymer‐Assisted Liquid–Liquid Phase Separation

Izri,

Noireaux

2024

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Living cells use liquid–liquid phase separation (LLPS) to compartmentalize metabolic functions into mesoscopic‐sized droplets. Deciphering the mechanisms at play in LLPS is therefore critical to understanding the structuration and functions of cells at the subcellular level. Although observed and achieved to a significant degree of control in vivo, the reconstitution of LLPS integrating advanced biological functions, such as gene expression, has been so far limited in vitro. LLPS of cell‐free transcription‐translation (TXTL) reactions require multi‐step experimental approaches that lack biomimetic and have relatively poor efficacy, thus limiting their usage in cell‐free engineered systems such as synthetic cells. Here the polymer‐assisted LLPS of TXTL reactions are reported as the single‐pot one‐step compartmentalization of a model complex metabolic system obtain without using solvents or surfactants. LLPS occurs by adding the biocompatible polymers poly(ethylene glycol), poly(vinyl alcohol), and dextran to a TXTL reaction, that remains highly active. These polymers serve as partitioning agents that localize TXTL in mesoscopic‐sized droplets rich in dextran. Cytoplasmic and membrane‐interacting proteins are synthesized preferentially inside these droplets, and localize either uniformly or preferentially at the interface, depending on their nature. The LLPS‐TXTL system presented in this work is a step toward the design of synthetic membraneless active organelles.

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Hydrogen Bond Arrangement Is Shown to Differ in Coexisting Phases of Aqueous Two-Phase Systems

Cited by 7 publications

References 37 publications

Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins

Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins

Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins

Membraneless Compartmentalization of Cell‐Free Transcription‐Translation by Polymer‐Assisted Liquid–Liquid Phase Separation

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