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Enthalpy vs Entropy Driven Complexation of Homoallylic Alcohols by Rh(I) Complexes.

ABSTRACT: The thermodynamics of binding between several homoallylic alcohols and simple olefinic Rh(I) compounds was examined with (1)H NMR spectroscopy and ITC. (1)H NMR titrations revealed moderate binding of these alcohols with [Rh(COD)(2)](+) (1) and [Rh(COD)(CH(3)CN)(2)](+) (3), but weaker binding with [Rh(NBD)(2)](+) (2). ITC indicated that the complexation with [Rh(COD)(2)](+) is mainly governed by enthalpy whereas binding with [Rh(COD)(CH(3)CN)(2)](+) is entirely driven by entropy. The thermodynamic parameters for the homoallylic alcohol binding of Rh(I) complexes 1-3 are consistent with crystallographic data.

SUBMITTER: Kang SO

PROVIDER: S-EPMC3274780 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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Enthalpy vs Entropy Driven Complexation of Homoallylic Alcohols by Rh(I) Complexes.

Kang Sung Ok SO Lynch Vincent M VM Day Victor W VW Anslyn Eric V EV

Organometallics 20111001 22

The thermodynamics of binding between several homoallylic alcohols and simple olefinic Rh(I) compounds was examined with (1)H NMR spectroscopy and ITC. (1)H NMR titrations revealed moderate binding of these alcohols with [Rh(COD)(2)](+) (1) and [Rh(COD)(CH(3)CN)(2)](+) (3), but weaker binding with [Rh(NBD)(2)](+) (2). ITC indicated that the complexation with [Rh(COD)(2)](+) is mainly governed by enthalpy whereas binding with [Rh(COD)(CH(3)CN)(2)](+) is entirely driven by entropy. The thermodynam ...[more]

PMID: 22328800

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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

Enthalpy vs Entropy Driven Complexation of Homoallylic Alcohols by Rh(I) Complexes.

Publications

Enthalpy vs Entropy Driven Complexation of Homoallylic Alcohols by Rh(I) Complexes.

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