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• W2011246315 abstract "Biomolecular functions are determined by their interactions with other molecules. Biomolecular recognition is often flexible and associated with large conformational changes involving both binding and folding. However, the global and physical understanding for the process is still challenging. Here, we quantified the intrinsic energy landscapes of flexible biomolecular recognition in terms of binding-folding dynamics for 15 homodimers by exploring the underlying density of states, using a structure-based model both with and without considering energetic roughness. By quantifying three individual effective intrinsic energy landscapes (one for interfacial binding, two for monomeric folding), the association mechanisms for flexible recognition of 15 homodimers can be classified into two-state cooperative coupled binding-folding and three-state noncooperative folding prior to binding scenarios. We found that the association mechanism of flexible biomolecular recognition relies on the interplay between the underlying effective intrinsic binding and folding energy landscapes. By quantifying the whole global intrinsic binding-folding energy landscapes, we found strong correlations between the landscape topography measure Λ (dimensionless ratio of energy gap versus roughness modulated by the configurational entropy) and the ratio of the thermodynamic stable temperature versus trapping temperature, as well as between Λ and binding kinetics. Therefore, the global energy landscape topography determines the binding-folding thermodynamics and kinetics, crucial for the feasibility and efficiency of realizing biomolecular function. We also found U-shape temperature-dependent kinetic behavior and a dynamical cross-over temperature for dividing exponential and nonexponential kinetics for two-state homodimers. Our study provides a unique way to bridge the gap between theory and experiments." @default.
• W2011246315 created "2016-06-24" @default.
• W2011246315 creator A5013799893 @default.
• W2011246315 creator A5018244700 @default.
• W2011246315 creator A5068298385 @default.
• W2011246315 creator A5072626733 @default.
• W2011246315 date "2013-06-10" @default.
• W2011246315 modified "2023-10-02" @default.
• W2011246315 title "Quantifying the topography of the intrinsic energy landscape of flexible biomolecular recognition" @default.
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• W2011246315 doi "https://doi.org/10.1073/pnas.1220699110" @default.
• W2011246315 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3696809" @default.
• W2011246315 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23754431" @default.
• W2011246315 hasPublicationYear "2013" @default.
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• W2011246315 hasAuthorship W2011246315A5068298385 @default.

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