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- W2040679209 endingPage "408" @default.
- W2040679209 startingPage "403" @default.
- W2040679209 abstract "Recent advances in NMR methods now allow protein complexes to be studied in great detail in a wide range of solution conditions. Isotope-enrichment strategies, resonance-assignment approaches and structural-determination methods have evolved to the point where almost any type of complex involving proteins of reasonable size may be studied in a straigthforward way. A variety of isotope editing and filtering strategies underlie these powerful methodologies. Approaches to the characterization of the dynamics of protein complexes have also matured to the point where detailed studies of the effects of complexation on dynamics can be studied over a wide range of timescales." @default.
- W2040679209 created "2016-06-24" @default.
- W2040679209 creator A5042370670 @default.
- W2040679209 creator A5081320421 @default.
- W2040679209 date "1996-08-01" @default.
- W2040679209 modified "2023-10-07" @default.
- W2040679209 title "Protein complexes studied by NMR spectroscopy" @default.
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