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• W1539341010 abstract "Biologically relevant macromolecules, such as proteins, do not operate as static, isolated entities. On the contrary, they are involved in numerous interactions with other species, such as proteins, nucleic acid, membranes, small molecule ligands, and also, critically, solvent molecules. These interactions often display a remarkable degree of specificity and high affinity. Fundamentally, the biological processes rely on molecular organisation and recognition events. Binding between two interacting partners has both enthalpic (H) and entropic (-TS) components, which means the recognition event is associated with changes of both the structure and dynamics of each counterpart. Like any other spontaneous process, binding occurs only when it is associated with a negative Gibbs' free energy of binding ( G  ), which may have differing thermodynamic signatures, varying from enthalpyto entropy-driven. Thus, the understanding of the forces driving the recognition and interaction require a detailed description of the binding thermodynamics, and a correlation of the thermodynamic parameters with the structures of interacting partners. Such an understanding of the nature of the recognition phenomena is of a great importance for medicinal chemistry and material research, since it enables truly rational structure-based molecular design. This chapter is organised in the following way. The first part of it introduces general principles which govern macromolecular associations under equilibrium conditions: the free energy of binding and its enthalpic and entropic components, the contributions from both interacting partners, interaction energy of the association, and specific types of interactions – such as hydrogen bonding or van der Waals interactions, ligand and protein flexibility, and ultimately solvent effects (e.g. solute-solvent interactions, solvent reorganisation). The second part is dedicated to methods applied to assess particular contributions, experimental as well as computational. Specifically, there will be a focus on isothermal titrational calorimetry (ITC), solution nuclear magnetic resonance (NMR), and a discussion of computational approaches to the estimation of enthalpic and entropic contributions to the binding free energy. I will discuss the applicability of these methods, the approximations behind them, and their limitations. In the third part of this chapter, I will provide the reader several examples of ligand-protein interactions and focus on the forces driving the associations, which can be very different from case to case. Finally, I will address several practical aspects of assessing the thermodynamic parameters in molecular design, the" @default.
• W1539341010 created "2016-06-24" @default.
• W1539341010 creator A5055986643 @default.
• W1539341010 date "2011-11-02" @default.
• W1539341010 modified "2023-10-10" @default.
• W1539341010 title "Thermodynamics of Ligand-Protein Interactions: Implications for Molecular Design" @default.
• W1539341010 cites W1481557920 @default.
• W1539341010 cites W1482516139 @default.
• W1539341010 cites W1482788902 @default.
• W1539341010 cites W1492262300 @default.
• W1539341010 cites W1548914255 @default.
• W1539341010 cites W1564376468 @default.
• W1539341010 cites W1596228091 @default.
• W1539341010 cites W1596745037 @default.
• W1539341010 cites W1964554313 @default.
• W1539341010 cites W1966438336 @default.
• W1539341010 cites W1966689737 @default.
• W1539341010 cites W1968739541 @default.
• W1539341010 cites W1969231606 @default.
• W1539341010 cites W1969479270 @default.
• W1539341010 cites W1970316689 @default.
• W1539341010 cites W1972629682 @default.
• W1539341010 cites W1974956783 @default.
• W1539341010 cites W1976160537 @default.
• W1539341010 cites W1976161355 @default.
• W1539341010 cites W1976949015 @default.
• W1539341010 cites W1980316342 @default.
• W1539341010 cites W1980337077 @default.
• W1539341010 cites W1980945455 @default.
• W1539341010 cites W1981049088 @default.
• W1539341010 cites W1981154770 @default.
• W1539341010 cites W1981673862 @default.
• W1539341010 cites W1981750741 @default.
• W1539341010 cites W1982648945 @default.
• W1539341010 cites W1985445693 @default.
• W1539341010 cites W1985767604 @default.
• W1539341010 cites W1986814683 @default.
• W1539341010 cites W1987759430 @default.
• W1539341010 cites W1988703094 @default.
• W1539341010 cites W1992165105 @default.
• W1539341010 cites W1992218453 @default.
• W1539341010 cites W1993248675 @default.
• W1539341010 cites W1995818918 @default.
• W1539341010 cites W1997738444 @default.
• W1539341010 cites W1997947637 @default.
• W1539341010 cites W1998501624 @default.
• W1539341010 cites W1998643862 @default.
• W1539341010 cites W1998948060 @default.
• W1539341010 cites W1999621555 @default.
• W1539341010 cites W1999798503 @default.
• W1539341010 cites W2001703421 @default.
• W1539341010 cites W2002111217 @default.
• W1539341010 cites W2004473597 @default.
• W1539341010 cites W2004761595 @default.
• W1539341010 cites W2005005853 @default.
• W1539341010 cites W2005087735 @default.
• W1539341010 cites W2008282292 @default.
• W1539341010 cites W2015647379 @default.
• W1539341010 cites W2015805666 @default.
• W1539341010 cites W2016271327 @default.
• W1539341010 cites W2016901528 @default.
• W1539341010 cites W2017498896 @default.
• W1539341010 cites W2019813447 @default.
• W1539341010 cites W2025373748 @default.
• W1539341010 cites W2025717854 @default.
• W1539341010 cites W2026968105 @default.
• W1539341010 cites W2028329272 @default.
• W1539341010 cites W2029205363 @default.
• W1539341010 cites W2034185634 @default.
• W1539341010 cites W2035199159 @default.
• W1539341010 cites W2036668937 @default.
• W1539341010 cites W2049592631 @default.
• W1539341010 cites W2052279034 @default.
• W1539341010 cites W2053499564 @default.
• W1539341010 cites W2055125957 @default.
• W1539341010 cites W2055141456 @default.
• W1539341010 cites W2055420034 @default.
• W1539341010 cites W2055563809 @default.
• W1539341010 cites W2056042508 @default.
• W1539341010 cites W2056309239 @default.
• W1539341010 cites W2056640340 @default.
• W1539341010 cites W2057309818 @default.
• W1539341010 cites W2065057333 @default.
• W1539341010 cites W2066951434 @default.
• W1539341010 cites W2069586413 @default.
• W1539341010 cites W2069777400 @default.
• W1539341010 cites W2073685932 @default.
• W1539341010 cites W2073775843 @default.
• W1539341010 cites W2075677721 @default.
• W1539341010 cites W2075828031 @default.
• W1539341010 cites W2079318633 @default.
• W1539341010 cites W2079495753 @default.
• W1539341010 cites W2081719547 @default.
• W1539341010 cites W2082308337 @default.
• W1539341010 cites W2087812229 @default.
• W1539341010 cites W2088636096 @default.
• W1539341010 cites W2089019157 @default.
• W1539341010 cites W2091408495 @default.
• W1539341010 cites W2094605637 @default.
• W1539341010 cites W2097859179 @default.

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