Marina Katava

Marina Katava
French National Centre for Scientific Research | CNRS · Institut de Biologie Physico-Chimique

About

12
Publications
713
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139
Citations

Publications

Publications (12)
Article
In multicellular organisms, nucleosomes carry epigenetic information that defines distinct patterns of gene expression, which are inherited over multiple generations. The enhanced capacity for information storage arises by nucleosome modifications, are triggered by enzymes. Modified nucleosomes can transfer the mark to others that are in proximity...
Preprint
In multicellular organisms, nucleosomes, the building blocks of chromatin, carry epigenetic information, defining distinct patterns of gene expression, that are inherited over many generations. The enhanced capacity for information storage arises by modification of nucleosomes triggered by specific enzymes. Nucleosomes in a modified state can trans...
Article
In this work we combine experiments and molecular simulations to unveil the hidden allosteric propensity of a thermophilic malate dehydrogenase protein (MDH). We provide evidence that at its working temperature the non-allosteric MDH takes a compact structure because of internal dewetting, and reorganizes the active state toward functional conforma...
Article
Internal subnanosecond timescale motions are key for the function of proteins, and are coupled to the surrounding solvent environment. These fast fluctuations guide protein conformational changes, yet their role for protein stability, and for unfolding, remains elusive. Here, in analogy with the Lindemann criterion for the melting of solids, we dem...
Article
We introduce a novel strategy to quantify the disorder of extended water-water hydrogen-bond (HB) networks sampled in particle-based computer simulations. The method relies on the conformational clustering of the HB connectivity states. We successfully applied it to unveil the fine relationship among the protein dynamical transition in hydrated pow...
Article
Full-text available
Conformational changes occurring during the enzymatic turnover are essential for the regulation of protein functionality. Individuating the protein regions involved in these changes and the associated mechanical modes is still a challenge at both experimental and theoretical levels. We present here a detailed investigation of the thermal activation...
Article
Comparing homologous enzymes adapted to different thermal environments aids to shed light on their delicate stability/function trade-off. Protein mechanical rigidity was postulated to secure stability and high-temperature functionality of thermophilic proteins. In this work we challenge the corresponding-state principle for a pair of homologous GTP...
Article
Full-text available
Our work focuses on determining the effect of crowded environment and different solvents on the thermal stability of the protein Lysozyme [1] placed in a dilute water solution, dehydrated protein powder, and in a protein powder glycerol solution, the latter two representing crowded environments.The ultimate goal of our work is to probe the validity...
Article
Micron-sized anisotropic particles with homogeneous surface properties at a fluid interface can deform the interface due to their shape. The particles thereby create excess interfacial area and interact in order to minimize this area, which lowers the total interfacial energy. We present a systematic investigation of the interface deformations arou...

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