ArticleJournal of biological physics2010
Mean-squared atomic displacements in hydrated lysozyme, native and denatured.
Article in Journal of biological physics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Decoupling of the onset of anharmonicity between a protein and its surface water around 200 K.eLife · 2024Article
- Dynamics of lysozyme and its hydration water under an electric field.Journal of biological physics · 2014Article
- Dynamical coupling of intrinsically disordered proteins and their hydration water: comparison with folded soluble and membrane proteins.Biophysical journal · 2012Article
- Mechanistic insight into the structure and dynamics of entangled and hydrated λ-phage DNA.The journal of physical chemistry. A · 2012Article
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Authors and funding
3 authors.
Funding
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Abstract
We use elastic neutron scattering to demonstrate that a sharp increase in the mean-squared atomic displacements, commonly observed in hydrated proteins above 200 K and often referred to as the dynamical transition, is present in the hydrated state of both native and denatured lysozyme. A direct comparison of the native and denatured protein thus confirms that the presence of the transition in the mean-squared atomic displacements is not specific to biologically functional molecules.
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