Dataset Information

Disordered enthalpy-entropy descriptor for high-entropy ceramics discovery.

ABSTRACT: The need for improved functionalities in extreme environments is fuelling interest in high-entropy ceramics^1-3. Except for the computational discovery of high-entropy carbides, performed with the entropy-forming-ability descriptor⁴, most innovation has been slowly driven by experimental means^1-3. Hence, advancement in the field needs more theoretical contributions. Here we introduce disordered enthalpy-entropy descriptor (DEED), a descriptor that captures the balance between entropy gains and enthalpy costs, allowing the correct classification of functional synthesizability of multicomponent ceramics, regardless of chemistry and structure. To make our calculations possible, we have developed a convolutional algorithm that drastically reduces computational resources. Moreover, DEED guides the experimental discovery of new single-phase high-entropy carbonitrides and borides. This work, integrated into the AFLOW computational ecosystem, provides an array of potential new candidates, ripe for experimental discoveries.

SUBMITTER: Divilov S

PROVIDER: S-EPMC10764291 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Disordered enthalpy-entropy descriptor for high-entropy ceramics discovery.

Divilov Simon S Eckert Hagen H Hicks David D Oses Corey C Toher Cormac C Friedrich Rico R Esters Marco M Mehl Michael J MJ Zettel Adam C AC Lederer Yoav Y Zurek Eva E Maria Jon-Paul JP Brenner Donald W DW Campilongo Xiomara X Filipović Suzana S Fahrenholtz William G WG Ryan Caillin J CJ DeSalle Christopher M CM Crealese Ryan J RJ Wolfe Douglas E DE Calzolari Arrigo A Curtarolo Stefano S

Nature 20240103 7993

The need for improved functionalities in extreme environments is fuelling interest in high-entropy ceramics1-3. Except for the computational discovery of high-entropy carbides, performed with the entropy-forming-ability descriptor4, most innovation has been slowly driven by experimental means1-3. Hence, advancement in the field needs more theoretical contributions. Here we introduce disordered enthalpy-entropy descriptor (DEED), a descriptor that captures the bal ...[more]

PMID: 38172364

Similar Datasets

Project description:Exploring the protein-folding problem has been a longstanding challenge in molecular biology and biophysics. Intramolecular hydrogen (H)-bonds play an extremely important role in stabilizing protein structures. To form these intramolecular H-bonds, nascent unfolded polypeptide chains need to escape from hydrogen bonding with surrounding polar water molecules under the solution conditions that require entropy-enthalpy compensations, according to the Gibbs free energy equation and the change in enthalpy. Here, by analyzing the spatial layout of the side-chains of amino acid residues in experimentally determined protein structures, we reveal a protein-folding mechanism based on the entropy-enthalpy compensations that initially driven by laterally hydrophobic collapse among the side-chains of adjacent residues in the sequences of unfolded protein chains. This hydrophobic collapse promotes the formation of the H-bonds within the polypeptide backbone structures through the entropy-enthalpy compensation mechanism, enabling secondary structures and tertiary structures to fold reproducibly following explicit physical folding codes and forces. The temperature dependence of protein folding is thus attributed to the environment dependence of the conformational Gibbs free energy equation. The folding codes and forces in the amino acid sequence that dictate the formation of β-strands and α-helices can be deciphered with great accuracy through evaluation of the hydrophobic interactions among neighboring side-chains of an unfolded polypeptide from a β-strand-like thermodynamic metastable state. The folding of protein quaternary structures is found to be guided by the entropy-enthalpy compensations in between the docking sites of protein subunits according to the Gibbs free energy equation that is verified by bioinformatics analyses of a dozen structures of dimers. Protein folding is therefore guided by multistage entropy-enthalpy compensations of the system of polypeptide chains and water molecules under the solution conditions.

Dataset Information

Disordered enthalpy-entropy descriptor for high-entropy ceramics discovery.

Publications

Disordered enthalpy-entropy descriptor for high-entropy ceramics discovery.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets