NMR Methods to Characterize Protein-Ligand Interactions
نویسندگان
چکیده
منابع مشابه
Studies of protein-ligand interactions by NMR.
Solution-state NMR has become an accepted method for studying the structure of small proteins in solution. This has resulted in over 3000 NMR-based co-ordinate sets being deposited in the Protein Databank. It is becoming increasingly apparent, however, that NMR is also a very powerful tool for accessing interactions between macromolecules and various ligands. These interactions can be assessed ...
متن کامل[Methods for analysis of protein-protein and protein-ligand interactions].
In order to maintain cellular homeostasis, cellular proteins coexist in complex and variable molecular assemblies. Therefore, understanding of major physiological processes at molecular level is based on analysis of protein-protein interaction networks. Firstly, composition of the molecular assembly has to be qualitatively analyzed. In the next step, quantitative bio-chemical properties of the ...
متن کاملQuantitative analysis of protein-ligand interactions by NMR.
Protein-ligand interactions have been commonly studied through static structures of the protein-ligand complex. Recently, however, there has been increasing interest in investigating the dynamics of protein-ligand interactions both for fundamental understanding of the underlying mechanisms and for drug development. NMR is a versatile and powerful tool, especially because it provides site-specif...
متن کاملNMR-based structural characterization of large protein-ligand interactions.
Genomic research on target identification and validation has created a great need for methods that rapidly provide detailed structural information on protein-ligand interactions. We developed a suite of NMR experiments as rapid and efficient tools to provide descriptive structural information on protein-ligand complexes. The methods work with large proteins and in particular cases also without ...
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ژورنال
عنوان ژورنال: Natural Product Communications
سال: 2019
ISSN: 1934-578X,1555-9475
DOI: 10.1177/1934578x19849296