Dataset Information

Molar Entropy and Enthalpy of CO Adsorbed in Zeolites as Derived from VTIR Data: Role of Intermolecular Modes.

ABSTRACT: Detailed analysis of recently reported variable-temperature IR (VTIR) spectra of carbon monoxide adsorbed in alkaline zeolites shows how, not only the corresponding values of standard adsorption enthalpy ( ?H0 ) and entropy ( ?S0 ) can be obtained, but also the thermodynamic values of molar entropy and enthalpy which characterize the adsorbed gas phase. In addition, it is shown that the so obtained molar entropy data can lead to new insights into soft molecular modes, which would be hardly accessible by conventional IR spectroscopic techniques.

SUBMITTER: Garrone E

PROVIDER: S-EPMC7239313 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature

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Molar Entropy and Enthalpy of CO Adsorbed in Zeolites as Derived from VTIR Data: Role of Intermolecular Modes.

Garrone Edoardo E Otero Areán Carlos C Rodríguez Delgado Montserrat M Bonelli Barbara B

ChemistryOpen 20200520 5

Detailed analysis of recently reported variable-temperature IR (VTIR) spectra of carbon monoxide adsorbed in alkaline zeolites shows how, not only the corresponding values of standard adsorption enthalpy ( ΔH0 ) and entropy ( ΔS0 ) can be obtained, but also the thermodynamic values of molar entropy and enthalpy which characterize the adsorbed gas phase. In addition, it is shown that the so obtained molar entropy data can lead to new insights into soft molecular modes, which would be hardly acces ...[more]

PMID: 32440464

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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

Molar Entropy and Enthalpy of CO Adsorbed in Zeolites as Derived from VTIR Data: Role of Intermolecular Modes.

Publications

Molar Entropy and Enthalpy of CO Adsorbed in Zeolites as Derived from VTIR Data: Role of Intermolecular Modes.

Similar Datasets

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