Literature DB >> 12670658

Allosteric interactions and QSAR: on the role of ligand hydrophobicity.

Corwin Hansch1, Rajni Garg, Alka Kurup, Suresh Babu Mekapati.   

Abstract

A study of a very large database of QSAR (9100) has uncovered a few unusual examples where as one increases the hydrophobicity of the members of a set of congeners, activity decreases until at a certain point, activity begins to increase. Obviously a change in mechanism is involved. The only way we have found to rationalize this unusual event is by a change in the structure of the receptor. We have found this to occur with hemoglobin, a substance first used to define allosteric reactions.

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Year:  2003        PMID: 12670658     DOI: 10.1016/s0968-0896(03)00056-7

Source DB:  PubMed          Journal:  Bioorg Med Chem        ISSN: 0968-0896            Impact factor:   3.641


  2 in total

1.  Guanidinium derivatives bind preferentially and trigger long-distance conformational changes in an engineered T4 lysozyme.

Authors:  Mohammad S Yousef; Nicole Bischoff; Collin M Dyer; Walter A Baase; Brian W Matthews
Journal:  Protein Sci       Date:  2006-04       Impact factor: 6.725

2.  Outliers in SAR and QSAR: 4. effects of allosteric protein-ligand interactions on the classical quantitative structure-activity relationships.

Authors:  Ki Hwan Kim
Journal:  Mol Divers       Date:  2022-02-22       Impact factor: 3.364

  2 in total

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