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Seeing the Invisible by Solution NMR Spectroscopy
Author(s) -
Kay Lewis Edward
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a39-e
Subject(s) - folding (dsp implementation) , chemistry , nuclear magnetic resonance spectroscopy , protein folding , characterization (materials science) , ligand (biochemistry) , nanotechnology , materials science , stereochemistry , biochemistry , receptor , electrical engineering , engineering
Many biochemical processes proceed through the formation of functionally important intermediates. For example, ligand binding, enzyme catalysis and protein folding may all involve the formation of one or more intermediates along the reaction coordinate connecting the initial and final protein states. A complete understanding of each process, requires, therefore, characterization of these intermediates in detail. While methods exist for studying the endpoints of these processes at atomic resolution in many cases, similar studies of the intermediates remain elusive. NMR methods for seeing such ‘invisible’ states will be described, along with a number of applications to protein folding illustrating the power of the methodology. A related problem is one where ‘near invisible’ systems are studied by solution NMR, such as supra‐molecular structures, with molecular weights in the MDa range. New labeling approaches and NMR experiments will be described that bring such systems into focus and applications to the ClpP protease and the proteasome will be presented.