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).
KeywordsNuclear Magnetic Resonance Ternary Complex Dipolar Coupling Rotor Cycle Phosphonate Group
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- Archer SJ, Bax A, Roberts AB, Sporn MB, Ogawa Y, Piez KA, Weatherbee JA, Tsang ML-S, Lucas R, Zheng B-L, Wenker J, Torchia DA (1993) Transforming growth factor β1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells. Biochemistry 32: 1152–1163PubMedCrossRefGoogle Scholar
- Ghuysen J-M, Strominger JL, Tipper DJ (1968) Bacterial cell walls. In: Florkin M, Stotz EH (eds) Comprehensive biochemistry, vol 26A. Elsevier, Amsterdam, pp 53–104Google Scholar
- Gullion T, Schaefer J (1989a) Rotational-echo double-resonance NMR. J Magn Reson 81:196–200Google Scholar
- Gullion T, Baker DB, Conradi MS (1990) New, compensated Carr-Purcell sequences. J Magn Reson 89:479–484Google Scholar
- Labischinski H, Hochberg M, Sidow T, Maidhof H, Henze U, Berger-Bächi B, Weche J (1993) Biophysical and biochemical studies on the fine structure of the sacculi from Escherichia coli and Staphylococcus aureus. In: DePe-dro MA, Höltje JV, Löffelhardt W (eds) Bacterial growth and lysis: metabolism and structure of the bacterial sacculus. Plenum, New York, pp 9–21Google Scholar
- Stallings WC, Abdel-Meguid SS, Lim LW, Shieh H-S, Dayringer HE, Le-imgruber NK, Stegeman RA, Anderson KS, Sikorski JA, Padgette SR, Kishore GM (1991) Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold. Proc Natl Acad Sci USA 88:5046–5050PubMedCrossRefGoogle Scholar
- Stejskal EO, Memory JD (1994) High resolution NMR in solid state: fundamentals of CP/MAS. Oxford University Press, New York, p 65Google Scholar
- Williams DH (1996) The glycopeptide story — how to kill the deadly “super-bugs.” Nat Prod Rep 469–477Google Scholar