Enthalpy-entropy compensation in the thermodynamics of hydrophobicity

Lee, B.

doi:10.1016/0301-4622(94)00048-4

Cited by 200 publications

(109 citation statements)

References 19 publications

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“…This behavior is consistent with the presence of enthalpy-entropy compensation phenomena induced by changes in the network of electrostatic interactions within the hydration sphere of proteins [68][69][70][71][72][73][74] and a prevailing enthalpic stabilization of the oxidized form of the protein -attributable to the electrostatic effect of the negatively charged ionic atmosphere -can be proposed as being responsible for the negative value of DE 00 [49].…”

Section: Discussionsupporting

confidence: 77%

Redox thermodynamics of cytochrome c adsorbed on mercaptoundecanol monolayer electrodes

Gavioli

Borsari

Cannio

et al. 2004

Journal of Electroanalytical Chemistry

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Section: Discussionsupporting

confidence: 77%

Redox thermodynamics of cytochrome c adsorbed on mercaptoundecanol monolayer electrodes

Gavioli

Borsari

Cannio

et al. 2004

Journal of Electroanalytical Chemistry

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“…Thus, the simulations consistently probe the disruption of secondary structure in the laccase as a function of higher T corresponding to a shift of interactions from enthalpy-dominated to entropy-dominated, as the TΔS term is favored at higher T. Such entropy-enthalpy compensation is well-known experimentally [26], [27], [28], [68], [69] but is rarely quantified structurally. The quantification of a loss of ∼7 average hydrogen bonds per 50 K relates only to the chosen criteria [64].…”

Section: Resultsmentioning

confidence: 73%

Stability Mechanisms of a Thermophilic Laccase Probed by Molecular Dynamics

Christensen

Kepp

2013

PLoS ONE

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Laccases are highly stable, industrially important enzymes capable of oxidizing a large range of substrates. Causes for their stability are, as for other proteins, poorly understood. In this work, multiple-seed molecular dynamics (MD) was applied to a Trametes versicolor laccase in response to variable ionic strengths, temperatures, and glycosylation status. Near-physiological conditions provided excellent agreement with the crystal structure (average RMSD ∼0.92 Å) and residual agreement with experimental B-factors. The persistence of backbone hydrogen bonds was identified as a key descriptor of structural response to environment, whereas solvent-accessibility, radius of gyration, and fluctuations were only locally relevant. Backbone hydrogen bonds decreased systematically with temperature in all simulations (∼9 per 50 K), probing structural changes associated with enthalpy-entropy compensation. Approaching T opt (∼350 K) from 300 K, this change correlated with a beginning “unzipping” of critical β-sheets. 0 M ionic strength triggered partial denucleation of the C-terminal (known experimentally to be sensitive) at 400 K, suggesting a general salt stabilization effect. In contrast, F− (but not Cl−) specifically impaired secondary structure by formation of strong hydrogen bonds with backbone NH, providing a mechanism for experimentally observed small anion destabilization, potentially remedied by site-directed mutagenesis at critical intrusion sites. N-glycosylation was found to support structural integrity by increasing persistent backbone hydrogen bonds by ∼4 across simulations, mainly via prevention of F− intrusion. Hydrogen-bond loss in distinct loop regions and ends of critical β-sheets suggest potential strategies for laboratory optimization of these industrially important enzymes.

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“…It is well known that the enthalpy and entropy changes of such processes are strongly temperature-dependent, 56,57 and in many cases it is not easy to describe such dependencies in an exact mathematical form. Following approaches used in protein unfolding studies (applying Co-operative Binding Effects on Protein NH Exchange the Gibbs-Helmoltz equation as used for example by Fersht 58 ), one can express the temperature-dependence of protection factors as:…”

Section: Enthalpies and Entropies For Hydrogen Exchange Processesmentioning

confidence: 99%