Chemistry Reference
In-Depth Information
68. Hwang PM, Choy WY, Lo EI, Chen L, Forman-Kay JD, Raetz CR, Priv´ GG, Bishop RE,
Kay LE (2002) Solution structure and dynamics of the outer membrane enzyme PagP by
NMR. Proc Natl Acad Sci USA 99:13560-13565
69. Arora A, Abildgaard F, Bushweller JH, Tamm LK (2001) Structure of outer membrane
protein A transmembrane domain by NMR spectroscopy. Nat Struct Biol 8:334-338
70. Renault M, Saurel O, Czaplicki J, Demange P, Gervais V, Lohr F, R´at V, Piotto M, Milon A
(2009) Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane
domain possessing a high potential for immunological applications. J Mol Biol 385:117-130
71. Fern´ndez C, Hilty C, Wider G, Guntert P, Wuthrich K (2004) NMR structure of the integral
membrane protein OmpX. J Mol Biol 336:1211-1221
72. Liang B, Tamm LK (2007) Structure of outer membrane protein G by solution NMR
spectroscopy. Proc Natl Acad Sci USA 104:16140-16145
73. Hiller S, Garces RG, Malia TJ, Orekhov VY, Colombini M, Wagner G (2008) Solution
structure of the integral human membrane protein VDAC-1 in detergent micelles. Science
321:1206-1210
74. Park SH, Prytulla S, De Angelis AA, Brown JM, Kiefer H, Opella SJ (2006) High-resolution
NMR spectroscopy of a GPCR in aligned bicelles. J Am Chem Soc 128:7402-7403
75. Schmidt P, Berger C, Scheidt HA, Berndt S, Bunge A, Beck-Sickinger AG, Huster D (2010)
A reconstitution protocol for the in vitro folded human G protein-coupled Y-2 receptor into
lipid environment. Biophys Chem 150:29-36
76. Braiman MS, Stern LJ, Chao BH, Khorana HG (1987) Structure-function studies on bacteri-
orhodopsin. IV. Purification and renaturation of bacterio-opsin polypeptide expressed in
Escherichia coli . J Biol Chem 262:9271-9276
77. Jekabsons MB, Echtay KS, Arechaga I, Brand MD (2003) Molecular properties of purified
human uncoupling protein 2 refolded from bacterial inclusion bodies. J Bioenerg Biomembr
35:409-418
78. Pebay-Peyroula E, Dahout-Gonzalez C, Kahn R, Tr´z´guet V, Lauquin GJ, Brandolin G
(2003) Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside.
Nature 426:39-44
79. Kim DM, Choi CY (1996) A semicontinuous prokaryotic coupled transcription/translation
system using a dialysis membrane. Biotechnol Prog 12:645-649
80. Knapp KG, Swartz JR (2004) Cell-free production of active E. coli thioredoxin reductase and
glutathione reductase. FEBS Lett 559:66-70
81. Tyler RC, Aceti DJ, Bingman CA, Cornilescu CC, Fox BG, Frederick RO, Jeon WB, Lee MS,
Newman CS, Peterson FC, Phillips GN, Shahan MN, Singh S, Song J, Sreenath HK,
Tyler EM, Ulrich EL, Vinarov DA, Vojtik FC, Volkman BF, Wrobel RL, Zhao Q,
Markley JL (2005) Comparison of cell-based and cell-free protocols for producing target
proteins from the Arabidopsis thaliana genome for structural studies. Proteins 59:633-643
82. Vinarov DA, Lytle BL, Peterson FC, Tyler EM, Volkman BF, Markley JL (2004) Cell-free
protein production and labeling protocol for NMR-based structural proteomics. Nat Methods
1:149-153
83. Spirin AS (2004) High-throughput cell-free systems for synthesis of functionally active
proteins. Trends Biotechnol 22:538-545
84. Baranov VI, Spirin AS (1993) Gene-expression in cell-free system on preparative-scale.
Methods Enzymol 217:123-142
85. Koglin A, Klarnmt C, Trbovic N, Schwarz D, Schneider B, Schafer B, Lohr F, Bernhard F,
Dotsch V (2006) Combination of cell-free expression and NMR spectroscopy as a new
approach for structural investigation of membrane proteins. Magn Reson Chem 44:S17-S23
86. Kigawa T, Yabuki T, Yoshida Y, Tsutsui M, Ito Y, Shibata T, Yokoyama S (1999) Cell-free
production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett
442:15-19
87. Kigawa T, Muto Y, Yokoyama S (1995) Cell-free synthesis and amino acid-selective stable-
isotope labeling of proteins for NMR analysis. J Biomol NMR 6:129-134
Search WWH ::




Custom Search