ArticleProceedings of the National Academy of Sciences of the United States of America2011
Protein dynamical transition at 110 K.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Conformational flexibility of His200 enables catalytic activity in the T200H mutant of carbonic anhydrase II.Molecules and cells · 2025Article
- Fast product release requires active-site water dynamics in carbonic anhydrase.Nature communications · 2025Article
- Dependence of crystallographic atomic displacement parameters on temperature (25-150 K) for complexes of horse liver alcohol dehydrogenase.Acta crystallographica. Section D, Structural biology · 2022Article
- Direct observation of reversible liquid-liquid transition in a trehalose aqueous solution.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Fast Motions of Key Methyl Groups in Amyloid-β Fibrils.Biophysical journal · 2016Article
- Glass-to-cryogenic-liquid transitions in aqueous solutions suggested by crack healing.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The glassy state of crambin and the THz time scale protein-solvent fluctuations possibly related to protein function.BMC biophysics · 2014Article
- A high-pressure cryocooling method for protein crystals and biological samples with reduced background X-ray scatter.Journal of applied crystallography · 2013Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Proteins are known to undergo a dynamical transition at around 200 K but the underlying mechanism, physical origin, and relationship to water are controversial. Here we report an observation of a protein dynamical transition as low as 110 K. This unexpected protein dynamical transition precisely correlated with the cryogenic phase transition of water from a high-density amorphous to a low-density amorphous state. The results suggest that the cryogenic protein dynamical transition might be directly related to the two liquid forms of water proposed at cryogenic temperatures.
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