REDOR NMR of Biological Solids: From Protein Binding Sites to Bacterial Cell Walls
Details of the structure and dynamics of proteins, nucleic acids, and their complexes are commonly obtained from two sources: X-ray crystallography and solution-state nuclear magnetic resonance (NMR). However, some proteins and protein complexes crystallize poorly or not at all. Many of these same proteins are insoluble, or aggregate in solution, or exceed the effective molecular-weight limit for solution-state NMR. Such systems may be suitable for analysis by solid-state NMR (Griffiths and Griffin 1993; Smith et al. 1996; McDowell and Schaefer 1996).
KeywordsGlycine Lysine Arginine Glutamine Histidine
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