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.