Parallel change with temperature of water structure and protein behavior

Article Abstract:

The unfolding of proteins and ligand binding by proteins were widely observed in dome-shaped temperature dependencies. These curves have been highly rationalized in terms of hydrophobic interactions. Similar dependencies were also found for transfer equilibria of many nonpolar molecules to water and these have also been ascribed to hydrophobic effects. An equation for protein unfolding was derived from the adoption of a phenomenological formulation of unfolding transformations that coupled the conformational arrangement in a protein with forms of water.

Evaluation, Protein research, Temperature

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Ab initio fragment molecular orbital study of molecular interactions between liganded retinoid X receptor and its coactivator: Roles of helix 12 in the coactivator binding mechanism

Article Abstract:

The ab initio fragment molecular orbital (FMO) calculations are performed for molecular interactions between 9-cis-retinoic acid (9cRA) liganded retinoid X receptor (RXR) and steroid receptor co-activating factor-1 (SRC1) coactivator to examine how helix 12 (H12) and its highly conserved residues contributes to the coactivator binding of RXR. It is found that SRC1 is proved to be stabilized mainly by the interaction with H12.

Retinoids, Molecular orbitals

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Concentration profiles of individual species in coupled binding of two ligands by a receptor

Article Abstract:

The compact stoichiometric expressions are formulated for two ligands of the concentration profiles for all species in coupled binding by a receptor. Protein-ligand interactions, is also applicable to other interacting systems, including those of macromolecular assembly.

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