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Modeling the mechanical response of tetragonal lysozyme crystals
1Mechanical, Aerospace, and Nuclear Engineering Department, Rensselaer Polytechnic Institute, 110 Eighth St., Troy, New York 12180, USA.
Langmuir : the ACS Journal of Surfaces and Colloids
|December 31, 2009
Summary
This study models how temperature and humidity affect tetragonal lysozyme crystals. Increased temperature and water content soften protein crystals by reducing critical resolved shear stress.
Area of Science:
- Biophysics
- Materials Science
- Crystallography
Background:
- Understanding the mechanical properties of protein crystals is crucial for their application in biotechnology.
- Lysozyme crystals are a model system for studying protein crystal behavior.
- Environmental factors like temperature and humidity can significantly influence crystal mechanics.
Purpose of the Study:
- To investigate the temperature- and humidity-dependent mechanical response of tetragonal lysozyme crystals.
- To develop and calibrate a continuum-based crystal plasticity model for protein crystals.
- To understand the role of intracrystalline water in the mechanical behavior of lysozyme.
Main Methods:
- Utilized a continuum-based crystal plasticity model.
- Calibrated the model with existing experimental Vickers microhardness test data.
- Incorporated temperature and humidity effects into elastic constants and critical resolved shear stresses.
Main Results:
- Lysozyme crystal mechanical response is anisotropic and orientation-dependent.
- Crystals exhibit purely elastic behavior along the [110] direction and elastoplastic behavior along [100] and [212] directions.
- Increased temperature and intracrystalline water content lead to decreased critical resolved shear stress, causing crystal softening.
Conclusions:
- The developed crystal plasticity model accurately captures the mechanical response of lysozyme crystals under varying temperature and humidity.
- Environmental factors significantly influence the mechanical properties of protein crystals.
- The findings have implications for the design and application of protein crystals in biotechnology.

