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- W2061287918 abstract "Abstract The rate of drug discovery is greatly dependent on the development and improvement of rapid and reliable analytical methods that allow screening for protein–ligand interactions. The solution‐based methods for investigating protein–ligand interactions by mass spectrometry (MS), which are discussed in this paper, are hydrogen/deuterium exchange of protein backbone amide hydrogens, and photoaffinity labeling. Moreover, MS analysis of intact noncovalent protein–ligand complexes is described. Fourier transform ion cyclotron resonance mass spectrometry (FTICR–MS) with its ultra‐high resolution and excellent mass accuracy is also considered herein as it is gaining increasing popularity for a mass spectrometric investigation of protein–ligand interactions." @default.
- W2061287918 created "2016-06-24" @default.
- W2061287918 creator A5084158849 @default.
- W2061287918 date "2007-04-04" @default.
- W2061287918 modified "2023-10-16" @default.
- W2061287918 title "Investigation of Protein–Ligand Interactions by Mass Spectrometry" @default.
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- W2061287918 doi "https://doi.org/10.1002/cmdc.200600298" @default.
- W2061287918 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17299828" @default.
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