Comparison of the internal dynamics of globular proteins in the microcrystalline and rehydrated lyophilized states

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1764, Issue 10, 2006, Pages 1639-1645

  Krushelnitsky, Alexey ^a   Gogolev, Yuri ^a   Golbik, Ralph ^b   Dahlquist, Frederick ^c   Reichert, Detlef ^b  

^a KAZAN INSTITUTE OF BIOCHEMISTRY AND BIOPHYSICS   (Russian Federation)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Dynamics; Microcrystals; Powders; Proteins; Solid state NMR

Indexed keywords

GLOBULAR PROTEIN; LYSOZYME; WATER;

ARTICLE; BACTERIOPHAGE; CONFORMATION; CRYSTALLIZATION; FREEZE DRYING; HEN; HYDRATION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REHYDRATION; SOLID STATE;

ANIMALS; BACTERIAL PROTEINS; CRYSTALLIZATION; CRYSTALLOGRAPHY; FREEZE DRYING; MURAMIDASE; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; VIRAL PROTEINS;

EID: 33749997243     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2006.08.015     Document Type: Article

References (36)

1. McDermott A.E. Structural and dynamic studies of proteins by solid-state NMR spectroscopy: rapid movement forward. Curr. Opin. Struct. Biol. 14 (2004) 554-561
2. Hughes C.E., and Baldus M. Magic-angle-spinning solid-state NMR applied to polypeptides and proteins. Annu. Rep. NMR Spectrosc. 55 (2005) 121-158
3. Wuthrich K. NMR-This other method for protein and nucleic-acid structure determination. Acta Crystallogr., D Biol. Crystallogr. 51 (1995) 249-270
4. Cole H.B.R., and Torchia D.A. An NMR study of the backbone dynamics of staphylococcal nuclease in the crystalline state. Chem. Phys. 158 (1991) 271-281
5. Seidel K., Etzkorn M., Heise H., Becker S., and Baldus M. High-resolution solid-state NMR studies on uniformly [C-13,N-15]-labeled ubiquitin. ChemBioChem 6 (2005) 1638-1647
6. Paulson E.K., Morcombe C.R., Gaponenko V., Dancheck B., Byrd R.A., and Zilm K.W. Sensitive high resolution inverse detection NMR spectroscopy of proteins in the solid state. J. Am. Chem. Soc. 125 (2003) 15831-15836
7. 15N chemical shift used as structural fingerprints. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 6362-6365
8. McDermott A., Polenova T., Bockmann A., Zilm K.W., Paulsen E.K., Martin R.W., and Montelione G.T. Partial NMR assignments for uniformly (C-13, N-15)-enriched BPTI in the solid state. J. Biomol. NMR 16 (2000) 209-219
9. Castellani F., van Rossum B., Diehl A., Schubert M., Rehbein K., and Oschkinat H. Structure of a protein determined by solid-state magic-angle-spinning NMR spectroscopy. Nature 420 (2002) 98-102
10. Bockmann A., Lange A., Galinier A., Luca S., Giraud N., Juy M., Heise H., Montserret R., Penin F., and Baldus M. Solid state NMR sequential resonance assignments and conformational analysis of the 2 × 10.4 kDa dimeric form of the Bacillus subtilis protein Crh. J. Biomol. NMR 27 (2003) 323-339
11. Rupley J.A., and Careri G. Protein hydration and function. Adv. Protein Chem. 41 (1991) 37-172
12. Krushelnitsky A., and Reichert D. Solid-state NMR and protein dynamics. Prog. Nucl. Magn. Reson. Spectrosc. 47 (2005) 1-25
13. Tamura A., Matsushita M., Naito A., Kojima S., Miura K.I., and Akasaka K. Dynamics of the three methionyl side chains of Streptomyces subtilisin inhibitor. Deuterium NMR studies in solution and in the solid state. Protein Sci. 5 (1996) 127-139
14. 15N NMR resonances of bacteriophage T4 lysozyme. Biochemistry 29 (1990) 6341-6362
15. Golbik R., Fischer G., and Fersht A.R. Folding of barstar C40A/C82A/P27A and catalysis of the peptidyl-prolyl cis/trans isomerization by human cytosolic cyclophilin (Cyp18). Protein Sci. 8 (1999) 1505-1514
16. Grutter M.G., Weaver L.H., and Matthews B.W. Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?. Nature 303 (1983) 828-831
17. Rupley J.A., Gratton E., and Careri G. Water and globular-proteins. Trends Biochem. Sci. 8 (1983) 18-22
18. Raghunathan V., Khurana S., Gupta V., Khurana R., Udgaonkar J.B., and Salunke D.M. Crystallization and molecular packing analysis of barstar crystals. J. Mol. Biol. 243 (1994) 533-536
19. Matthews B.W., Dahlquist F.W., and Maynard A.Y. Crystallographic data for lysozyme from bacteriophage T4. J. Mol. Biol. 78 (1973) 575-576
20. Kam Z., Shore H.B., and Feher G. Crystallization of proteins. J. Mol. Biol. 123 (1978) 539-555
21. Martin R.W., and Zilm K.W. Preparation of protein nanocrystals and their characterization by solid state NMR. J. Magn. Reson. 165 (2003) 162-174
22. Weber P.C. Overview of protein crystallization methods. Methods Enzymol. 276 (1997) 13-22
23. 1 values by a method which suppresses artifacts. J. Magn. Reson. 30 (1978) 613-616
24. 1ρ experiment for heteronuclear dipolar relaxation. Solid State Nucl. Magn. Reson. 22 (2002) 423-438
25. Vanderhart D.L., and Garroway A.N. 13C NMR rotating frame relaxation in a solid with strongly coupled protons: polyethylene. J. Chem. Phys. 71 (1979) 2773-2787
26. Pauli J., van Rossum B., Forster H., de Groot H.J.M., and Oschkinat H. Sample optimization and identification of signal patterns of amino acid side chains in 2D RFDR spectra of the alpha-spectrin SH3 domain. J. Magn. Reson. 143 (2000) 411-416
27. 13C solids NMR. Biopolymers 29 (1990) 1801-1806
28. 13C-NMR spectroscopy. Biopolymers 33 (1993) 513-519
29. Perry A., Stypa M.P., Tenn B.K., and Kumashiro K.K. Solid-state C-13 NMR reveals effects of temperature and hydration on elastin. Biophys. J. 82 (2002) 1086-1095
30. 13C-NMR spectroscopy. Biopolymers 33 (1993) 1871-1876
31. Krushelnitsky A., Reichert D., Hempel G., Fedotov V., Schneider H., Yagodina L., and Schulga A. Superslow backbone protein dynamics as studied by 1D solid-state MAS exchange NMR spectroscopy. J. Magn. Reson. 138 (1999) 244-255
32. Krushelnitsky A.G., Hempel G., and Reichert D. Simultaneous processing of solid-state NMR relaxation and 1D-MAS exchange data: the backbone dynamics of free vs. binase-bound barstar. BBA-Proteins Proteomics 1650 (2003) 117-127
33. deAzevedo E.R., Kennedy S.B., and Hong M. Determination of slow motions in extensively isotopically labeled proteins by magic-angle-spinning C-13-detected N-15 exchange NMR. Chem. Phys. Lett. 321 (2000) 43-48
34. Huster D., Xiao L.S., and Hong M. Solid-state NMR investigation of the dynamics of the soluble and membrane-bound colicin Ia channel-forming domain. Biochemistry 40 (2001) 7662-7674
35. Schreiber C., Buckle A.M., and Fersht A.R. Stability and function-2 constraints in the evolution of barstar and other proteins. Structure 2 (1994) 945-951
36. Buckle A.M., Schreiber G., and Fersht A.R. Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-Å resolution. Biochemistry 33 (1994) 8878-8889