Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins

Version 1 : Received: 17 August 2022 / Approved: 18 August 2022 / Online: 18 August 2022 (03:25:26 CEST)

A peer-reviewed article of this Preprint also exists.

Titus, A.R.; Madeira, P.P.; Ferreira, L.A.; Belgovskiy, A.I.; Mann, E.K.; Mann, J.A., Jr.; Meyer, W.V.; Smart, A.E.; Uversky, V.N.; Zaslavsky, B.Y. Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins. Int. J. Mol. Sci. 2022, 23, 11381. Titus, A.R.; Madeira, P.P.; Ferreira, L.A.; Belgovskiy, A.I.; Mann, E.K.; Mann, J.A., Jr.; Meyer, W.V.; Smart, A.E.; Uversky, V.N.; Zaslavsky, B.Y. Arrangement of Hydrogen Bonds in Aqueous Solutions of Different Globular Proteins. Int. J. Mol. Sci. 2022, 23, 11381.

Abstract

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.

Keywords

Fourier Transform Infrared spectroscopy; water structure; hydrogen bonds; protein solution; solvent properties

Subject

Biology and Life Sciences, Biophysics

Comments (0)

We encourage comments and feedback from a broad range of readers. See criteria for comments and our Diversity statement.

Leave a public comment
Send a private comment to the author(s)
* All users must log in before leaving a comment
Views 0
Downloads 0
Comments 0
Metrics 0


×
Alerts
Notify me about updates to this article or when a peer-reviewed version is published.
We use cookies on our website to ensure you get the best experience.
Read more about our cookies here.