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Updated: May 18, 2026

Picometer-Precision Atomic Position Tracking through Electron Microscopy

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Published on: July 3, 2021

Intrinsic mean-square displacements in proteins.

Derya Vural¹, Henry R Glyde

¹Department of Physics and Astronomy, University of Delaware, Newark, Delaware 19716-2570, USA.

Physical Review. E, Statistical, Nonlinear, and Soft Matter Physics

|September 26, 2012

Summary

Neutron scattering experiments measure protein hydrogen

Area of Science:

Biophysics
Materials Science
Neutron Scattering

Background:

The thermal mean-square displacement (MSD) of hydrogen in proteins and hydration water is a key indicator of protein function.
Current neutron scattering methods for determining MSD are influenced by instrument energy resolution width.

Purpose of the Study:

To develop a novel method for accurately measuring the intrinsic MSD of hydrogen in proteins.
To obtain an MSD measurement that is independent of neutron scattering instrument resolution.

Main Methods:

A new model is proposed for fitting to resolution-broadened elastic incoherent structure factor or resolution-dependent MSD data.
The model incorporates the intrinsic MSD, instrument resolution width, and a rate constant for hydrogen motion.
The method was applied to literature data for heparan sulfate, ribonuclease A, and staphylococcal nuclease.

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Main Results:

The proposed method successfully extracts the intrinsic MSD (r(2)) of hydrogen in the studied proteins.
This intrinsic MSD is independent of the neutron scattering instrument's energy resolution.

Conclusions:

The developed method provides a more accurate determination of protein hydrogen MSD.
This advancement allows for a better understanding of protein dynamics and function through intrinsic MSD measurements.