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Synchrotron X-ray footprinting as a method to visualize water in proteins

The vast majority of biomolecular processes are controlled or facilitated by water interactions. In enzymes, regulatory proteins, membrane-bound receptors and ion-channels, water bound to functionally important residues creates hydrogen-bonding networks that underlie the mechanism of action of the m...

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Autores principales: Gupta, Sayan, Feng, Jun, Chan, Leanne Jade G., Petzold, Christopher J., Ralston, Corie Y.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5006651/
https://www.ncbi.nlm.nih.gov/pubmed/27577756
http://dx.doi.org/10.1107/S1600577516009024
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author Gupta, Sayan
Feng, Jun
Chan, Leanne Jade G.
Petzold, Christopher J.
Ralston, Corie Y.
author_facet Gupta, Sayan
Feng, Jun
Chan, Leanne Jade G.
Petzold, Christopher J.
Ralston, Corie Y.
author_sort Gupta, Sayan
collection PubMed
description The vast majority of biomolecular processes are controlled or facilitated by water interactions. In enzymes, regulatory proteins, membrane-bound receptors and ion-channels, water bound to functionally important residues creates hydrogen-bonding networks that underlie the mechanism of action of the macromolecule. High-resolution X-ray structures are often difficult to obtain with many of these classes of proteins because sample conditions, such as the necessity of detergents, often impede crystallization. Other biophysical techniques such as neutron scattering, nuclear magnetic resonance and Fourier transform infrared spectroscopy are useful for studying internal water, though each has its own advantages and drawbacks, and often a hybrid approach is required to address important biological problems associated with protein–water interactions. One major area requiring more investigation is the study of bound water molecules which reside in cavities and channels and which are often involved in both the structural and functional aspects of receptor, transporter and ion channel proteins. In recent years, significant progress has been made in synchrotron-based radiolytic labeling and mass spectroscopy techniques for both the identification of bound waters and for characterizing the role of water in protein conformational changes at a high degree of spatial and temporal resolution. Here the latest developments and future capabilities of this method for investigating water–protein interactions and its synergy with other synchrotron-based methods are discussed.
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spelling pubmed-50066512017-09-01 Synchrotron X-ray footprinting as a method to visualize water in proteins Gupta, Sayan Feng, Jun Chan, Leanne Jade G. Petzold, Christopher J. Ralston, Corie Y. J Synchrotron Radiat Feature Articles The vast majority of biomolecular processes are controlled or facilitated by water interactions. In enzymes, regulatory proteins, membrane-bound receptors and ion-channels, water bound to functionally important residues creates hydrogen-bonding networks that underlie the mechanism of action of the macromolecule. High-resolution X-ray structures are often difficult to obtain with many of these classes of proteins because sample conditions, such as the necessity of detergents, often impede crystallization. Other biophysical techniques such as neutron scattering, nuclear magnetic resonance and Fourier transform infrared spectroscopy are useful for studying internal water, though each has its own advantages and drawbacks, and often a hybrid approach is required to address important biological problems associated with protein–water interactions. One major area requiring more investigation is the study of bound water molecules which reside in cavities and channels and which are often involved in both the structural and functional aspects of receptor, transporter and ion channel proteins. In recent years, significant progress has been made in synchrotron-based radiolytic labeling and mass spectroscopy techniques for both the identification of bound waters and for characterizing the role of water in protein conformational changes at a high degree of spatial and temporal resolution. Here the latest developments and future capabilities of this method for investigating water–protein interactions and its synergy with other synchrotron-based methods are discussed. International Union of Crystallography 2016-07-27 /pmc/articles/PMC5006651/ /pubmed/27577756 http://dx.doi.org/10.1107/S1600577516009024 Text en © International Union of Crystallography 2016 http://journals.iucr.org/services/termsofuse.html This is an open-access article distributed under the terms described at http://journals.iucr.org/services/termsofuse.html.
spellingShingle Feature Articles
Gupta, Sayan
Feng, Jun
Chan, Leanne Jade G.
Petzold, Christopher J.
Ralston, Corie Y.
Synchrotron X-ray footprinting as a method to visualize water in proteins
title Synchrotron X-ray footprinting as a method to visualize water in proteins
title_full Synchrotron X-ray footprinting as a method to visualize water in proteins
title_fullStr Synchrotron X-ray footprinting as a method to visualize water in proteins
title_full_unstemmed Synchrotron X-ray footprinting as a method to visualize water in proteins
title_short Synchrotron X-ray footprinting as a method to visualize water in proteins
title_sort synchrotron x-ray footprinting as a method to visualize water in proteins
topic Feature Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5006651/
https://www.ncbi.nlm.nih.gov/pubmed/27577756
http://dx.doi.org/10.1107/S1600577516009024
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