ArticleJournal of the American Chemical Society2011
Protein-ligand interactions: thermodynamic effects associated with increasing nonpolar surface area.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Mutant-Selective Binding ofInternational journal of molecular sciences · 2026Article
- Accurate protein stability prediction for small domains using mega-scale experiments.bioRxiv : the preprint server for biology · 2026Article
- Computable properties of selected monomeric acylphloroglucinols with anticancer and/or antimalarial activities and first-approximation docking study.Journal of molecular modeling · 2025Article
- Synthesis and structural characterization of a monocarboxylic inhibitor for GRB2 SH2 domain.Bioorganic & medicinal chemistry letters · 2021Article
- Some thermodynamic effects of varying nonpolar surfaces in protein-ligand interactions.European journal of medicinal chemistry · 2020Article
- Spontaneous drying of non-polar deep-cavity cavitand pockets in aqueous solution.Nature chemistry · 2020Article
- Structural and functional properties of Grb2 SH2 dimer in CD28 binding.Biophysics and physicobiology · 2019Article
- Ca2+ binding induced sequential allosteric activation of sortase A: An example for ion-triggered conformational selection.PloS one · 2018Article
- Natural Products and Their Mimics as Targets of Opportunity for Discovery.The Journal of organic chemistry · 2017Article
- Protein-ligand interactions: probing the energetics of a putative cation-π interaction.Bioorganic & medicinal chemistry letters · 2014Article
- Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing the Length of an Alkyl Chain.ACS medicinal chemistry letters · 2013Article
- Multiple binding modes for palmitate to barley lipid transfer protein facilitated by the presence of proline 12.Protein science : a publication of the Protein Society · 2013Article
- Ligand-induced protein mobility in complexes of carbonic anhydrase II and benzenesulfonamides with oligoglycine chains.PloS one · 2013Article
- The unsolved "solved-problem" of protein folding.Journal of biomolecular structure & dynamics · 2013Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Thermodynamic parameters were determined for complex formation between the Grb2 SH2 domain and Ac-pTyr-Xaa-Asn derived tripeptides in which the Xaa residue is an α,α-cycloaliphatic amino acid that varies in ring size from three- to seven-membered. Although the six- and seven-membered ring analogs are approximately equipotent, binding affinities of those having three- to six-membered rings increase incrementally with ring size because increasingly more favorable binding enthalpies dominate increasingly less favorable binding entropies, a finding consistent with an enthalpy-driven hydrophobic effect. Crystallographic analysis reveals that the only significant differences in structures of the complexes are in the number of van der Waals contacts between the domain and the methylene groups in the Xaa residues. There is a positive correlation between buried nonpolar surface area and binding free energy and enthalpy, but not with ΔC(p). Displacing a water molecule from a protein-ligand interface is not necessarily reflected in a favorable change in binding entropy. These findings highlight some of the fallibilities associated with commonly held views of relationships of structure and energetics in protein-ligand interactions and have significant implications for ligand design.
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