ArticleBiophysical journal2011
Crowding induces differences in the diffusion of thermophilic and mesophilic proteins: a new look at neutron scattering results.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Multi-Conformation Monte Carlo: A Method for Introducing Flexibility in Efficient Simulations of Many-Protein Systems.The journal of physical chemistry. B · 2016Article
- How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain.The journal of physical chemistry. B · 2013Article
- Hot and crowded: new insights into the dynamics of thermophilic enzymes from multiscale modeling.Biophysical journal · 2011Article
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3 authors.
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Abstract
The dynamical basis underlying the increased thermal stability of thermophilic proteins remains uncertain. Here, we challenge the new paradigm established by neutron scattering experiments in solution, in which the adaptation of thermophilic proteins to high temperatures lies in the lower sensitivity of their flexibility to temperature changes. By means of a combination of molecular dynamics and Brownian dynamics simulations, we report a reinterpretation of those experiments and show evidence that under crowding conditions, such as in vivo, thermophilic and homolog mesophilic proteins have diffusional properties with different thermal behavior.
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