From X-ray crystallographic structure to intrinsic thermodynamics of protein–ligand binding using carbonic anhydrase isozymes as a model system

Vaida Paketurytė-Latvė,Alexey Smirnov,Elena Manakova,Lina Baranauskiene,Vytautas Petrauskas, Asta Zubrienė,Jurgita Matulienė,Virginija Dudutienė,Edita Čapkauskaitė,Audrius Zakšauskas, Janis Leitans,Saulius Gražulis,Kaspars Tars,Daumantas Matulis, Z.-J. Liu

IUCrJ（2024）

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摘要

Rational drug discovery and design require a deep understanding of the structure and thermodynamics of protein–ligand interactions. Here, the human carbonic anhydrase family of enzymes and their specific sulfonamide ligands are used to describe binding assays and crystal structures for understanding of protein–compound recognition principles.

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关键词

drug discovery,protein structure,molecular recognition,X-ray crystallography,intermolecular interactions,carbonic anhydrase isozymes,protein–ligand binding,intrinsic thermodynamics,binding assays

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