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Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
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Related Experiment Video

Updated: Dec 12, 2025

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

Published on: August 14, 2018

Conformational Stability and Dynamics in Crystals Recapitulate Protein Behavior in Solution.

Benedetta Maria Sala¹, Tanguy Le Marchand², Guido Pintacuda²

¹Dipartimento di Bioscienze, Università degli Studi di Milano, Milano, Italy.

Biophysical Journal

|August 8, 2020

Summary

Protein crystals accurately reflect solution behavior, showing similar dynamics and stability. This confirms crystals are valuable for studying protein unfolding and aggregation, including pathological hidden states.

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Last Updated: Dec 12, 2025

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

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Published on: August 14, 2018

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Published on: March 11, 2022

Area of Science:

Biophysics
Structural Biology
Protein Science

Background:

Proteins can retain function and flexibility in crystalline environments.
Amyloidogenic protein precursors' transient states correlate with pathology.
The relationship between in-crystal and in-solution protein behavior is not fully understood.

Purpose of the Study:

To investigate if biophysical properties of proteins in microcrystalline states mirror their solution behavior.
To compare the conformational dynamics and stability of β2-microglobulin in solution versus its microcrystalline form.

Main Methods:

Nuclear Magnetic Resonance (NMR) chemical shifts
Molecular Dynamics (MD) simulations
Fourier Transform Infrared (FTIR) spectroscopy

Main Results:

NMR and MD simulations confirmed that β2-microglobulin's conformational dynamics in crystals match solution dynamics.
FTIR analysis showed that protein thermal stability in crystals is consistent with solution studies.
Crystalline samples yielded better-resolved spectral components due to increased structural order.

Conclusions:

Protein stability and the presence of pathological hidden states in crystals parallel their behavior in solution.
Crystals serve as a valid platform for biophysical characterization of protein unfolding and aggregation.
This study validates the use of crystallo characterization for understanding protein dynamics and disease-related states.