Chemistry Reference
In-Depth Information
[33] Muchmore, S. W., Sattler, M., Liang, H., Meadows, R. P., Harlan, H. E., Yoon, H. S.,
Nettesheim, D., Chang, B. S., Thompson, C. B., Wong, S.-L., Ng, S.-C. and Fesik, S. W. (1996).
X-ray and NMR structure of human Bcl-x L , an inhibitor of programmed cell death. Nature 381 ,
335-341.
[34] Sattler, M., Liang, H., Nettesheim, D., Meadows, R. P., Harlan, J. E., Eberstadt, M., Yoon, H.
S., Shuker, S. B., Chang, B. S., Minn, A. J., Thompson, C. B. and Fesik, S. W. (1997). Structure
of Bcl-x L -Bak peptide complex: recognition between regulators of apoptosis. Science 275 ,
983-986.
[35] Metzler, W. J., Wittekind, M., Goldfarb, V., Mueller, L. and Farmer, B. T., II (1996). Incorpora-
tion of 1 H/ 13 C/ 15 N-{Ile,Leu,Val} into a perdeuterated 15 N-labeled protein: potential in structure
determination of large proteins by NMR. J. Am. Chem. Soc . 118 , 6800-6801.
[36] Rosen, M. K., Gardner, K. H., Willis, R. C., Parris, W. E., Pawson, T. and Kay, L. E. (1996).
Selective methyl group protonation of perdeuterated proteins. J. Mol. Biol . 263 , 627-636.
[37] Gardner, K. H., Rosen, M. K. and Kay, L. E. (1997). Global folds of highly deuterated, methyl-
protonated proteins by multidimensional NMR. Biochemistry 36 , 1389-1401.
[38] Goto, N. K., Gardner, K. H., Mueller, G. A., Willis, R. C. and Kay, L. E. (1999). A robust and
cost-effective method for the production of Val, Leu, Ile (1) methyl-protonated 15 N-,
13 C-,
2 H-labeled proteins. J. Biomol. NMR , 13 , 369-374.
[39] Constantine, K. L., Mueller, L., Goldfarb, V., Wittekind, M., Metzler, W. J., Yanchunas, J., Jr.,
Robertson, J. G., Malley, M. F., Friedrichs, M. S. and Farmer, B. T., II. (1997). Characterization of
NADP + binding to perdeuterated MurB: backbone atom NMR assignments and chemical-shift
changes. J. Mol. Biol. 267 , 1223-1246.
[40] Pellecchia, M., Meininger, D., Dong, Q., Chang, E., Jack, R. and Sem, D. S. (2002). NMR-based
structural characterization of large protein-ligand interactions. J. Biomol. NMR 22 , 165-173.
[41] Hajduk, P. J., Mack, J. C., Olejniczak, E. T., Park, C., Dandliker, P. J. and Beutel, B. A. (2004).
SOS-NMR: a saturation transfer NMR-based method for determining the structures of protein-
ligand complexes. J. Am. Chem. Soc . 126 , 2390-2398.
[42] Mueller, L. and Kumar, N. V. (1996). Multidimensional NMR of macromolecules. In NMR
Spectroscopy and Its Application to Biomedical Research , ed. S. S. Sarkar, Elsevier,Amsterdam,
pp. 85-157.
[43] Spector, S., Wang, M., Carp, S. A., Robblee, J., Hendsch, Z. S., Fairman, R., Tidor, B. and
Raleigh, D. P. (2000). Rational modification of protein stability by the mutation of charged
surface residues. Biochemistry 39 , 872-879.
[44] Eijsink, V. G. H., Bjork, A., Gaseidnes, S., Sirevag, R., Synstad, B., van den Burg, B. and
Vriend, G. (2004). Rational engineering of enzyme stability. J. Biotechnol. 113 , 105-120.
[45] Bommarius, A. S., Broering, J. M., Chaparro-Riggers, J. F. and Polizzi, K. M. (2006). High-
throughput screening for enhanced protein stability. Curr. Opin. Biotechnol. 17 , 606-610.
[46] Thompson, M. J. and Eisenberg, D. (1999). Transproteomic evidence of a loop-deletion
mechanism for enhancing protein thermostability. J. Mol. Biol . 290 , 595-604.
[47] Matthews, S. J. and Leatherbarrow, R. J. (1993). The use of osmolytes to facilitate protein NMR
spectroscopy. J. Biomol. NMR 3 , 597-600.
[48] Street, T. O., Bolen, D.W. and Rose, G. D. (2006). Amolecular mechanism for osmolyte-induced
protein stability. Proc. Natl Acad. Sci. USA 103 , 13997-14002.
[49] Wand, A. J., Ehrhardt, M. R. and Flynn, P. F. (1998). High-resolution NMR of encapsulated
proteins dissolved in low-viscosity fluids. Proc. Natl. Acad. Sci. USA 95 , 15299-15302.
[50] Peterson, R. W., Lefebvre, B. G. and Wand, A. J. (2005). High-resolution NMR studies of
encapsulated proteins in liquid ethane. J. Am. Chem. Soc. 127 , 10176-10177.
[51] Huse, M. and Kuriyan, J. (2002). The conformational plasticity of protein kinases. Cell 109 ,
275-282.
Search WWH ::




Custom Search