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Updated: Apr 19, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water

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Pf1 bacteriophage hydration by magic angle spinning solid-state NMR.

Ivan V Sergeyev¹, Salima Bahri¹, Loren A Day²

¹Department of Chemistry, Columbia University, 3000 Broadway, New York, New York 10027, USA.

The Journal of Chemical Physics

|December 16, 2014

Summary

This summary is machine-generated.

High-resolution spectroscopy revealed detailed internal and external hydration of the Pf1 virion. Water channels were identified within the hydrophobic capsid, offering new insights into virion structure and function.

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Area of Science:

Structural biology
Biophysics
Biochemistry

Background:

The Pf1 virion is a long, slender biological particle with a DNA core encased in a protein capsid.
Understanding the hydration shell is crucial for characterizing viral structure and dynamics.

Purpose of the Study:

To detail the internal and external hydration water of the Pf1 virion using advanced spectroscopic techniques.
To map the hydration surface and identify water pathways within the virion.

Main Methods:

High-resolution two- and three-dimensional heteronuclear correlation spectroscopy ((1)H-(13)C, (1)H-(15)N, and (1)H-(13)C-(13)C HETCOR).
Paramagnetic relaxation enhancement to distinguish internal and external water.
Mapping of spectroscopic contacts onto structural models.

Main Results:

Unambiguous assignment of HETCOR cross-peaks to 25 amino acid residues and DNA deoxyribose rings.
Identification of hydration water in contact with both DNA and capsid proteins.
Evidence for water "tunnels" through hydrophobic regions of the capsid.
Distinction between internal and external hydration water populations.

Conclusions:

Provides a comprehensive hydration surface map of the Pf1 virion, significantly refining previous studies.
Internal water may function as a localized magnetization reservoir for structural studies.
The findings reveal intricate water-protein and water-DNA interactions within the virion.