메뉴 건너뛰기




Volumn 20, Issue 6, 2012, Pages 1019-1027

Requirements on paramagnetic relaxation enhancement data for membrane protein structure determination by NMR

Author keywords

[No Author keywords available]

Indexed keywords

HALORHODOPSIN; MEMBRANE PROTEIN; MEMBRANE PROTEIN DSBB; MEMBRANE PROTEIN GLPG; UNCLASSIFIED DRUG;

EID: 84861980106     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.03.010     Document Type: Article
Times cited : (35)

References (37)
  • 1
    • 0034625121 scopus 로고    scopus 로고
    • Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data
    • Battiste, J.L., and Wagner, G. (2000). Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data. Biochemistry 39, 5355-5365.
    • (2000) Biochemistry , vol.39 , pp. 5355-5365
    • Battiste, J.L.1    Wagner, G.2
  • 2
    • 79961168437 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching
    • Berardi, M.J., Shih, W.M., Harrison, S.C., and Chou, J.J. (2011). Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching. Nature 476, 109-113.
    • (2011) Nature , vol.476 , pp. 109-113
    • Berardi, M.J.1    Shih, W.M.2    Harrison, S.C.3    Chou, J.J.4
  • 4
    • 0034875587 scopus 로고    scopus 로고
    • Evaluation of site-directed spin labeling for characterizing protein-ligand complexes using simulated restraints
    • Constantine, K.L. (2001). Evaluation of site-directed spin labeling for characterizing protein-ligand complexes using simulated restraints. Biophys. J. 81, 1275-1284.
    • (2001) Biophys. J. , vol.81 , pp. 1275-1284
    • Constantine, K.L.1
  • 8
    • 77953286311 scopus 로고    scopus 로고
    • Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy
    • Gautier, A., Mott, H.R., Bostock, M.J., Kirkpatrick, J.P., and Nietlispach, D. (2010). Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy. Nat. Struct. Mol. Biol. 17, 768-774.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 768-774
    • Gautier, A.1    Mott, H.R.2    Bostock, M.J.3    Kirkpatrick, J.P.4    Nietlispach, D.5
  • 9
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie, J.R., and Shortle, D. (1997). Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 268, 170-184.
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 10
    • 84863110091 scopus 로고    scopus 로고
    • Simultaneous singlestructure and bundle representation of protein NMR structures in torsion angle space
    • Gottstein, D., Kirchner, D.K., and Güntert, P. (2012). Simultaneous singlestructure and bundle representation of protein NMR structures in torsion angle space. J. Biomol. NMR 52, 351-364.
    • (2012) J. Biomol. NMR , vol.52 , pp. 351-364
    • Gottstein, D.1    Kirchner, D.K.2    Güntert, P.3
  • 11
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997). Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 12
    • 50649121583 scopus 로고    scopus 로고
    • Solution structure of the integral human membrane protein VDAC-1 in detergent micelles
    • Hiller, S., Garces, R.G., Malia, T.J., Orekhov, V.Y., Colombini, M., and Wagner, G. (2008). Solution structure of the integral human membrane protein VDAC-1 in detergent micelles. Science 321, 1206-1210.
    • (2008) Science , vol.321 , pp. 1206-1210
    • Hiller, S.1    Garces, R.G.2    Malia, T.J.3    Orekhov, V.Y.4    Colombini, M.5    Wagner, G.6
  • 13
    • 2442433447 scopus 로고    scopus 로고
    • Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule
    • Iwahara, J., Schwieters, C.D., and Clore, G.M. (2004). Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule. J. Am. Chem. Soc. 126, 5879-5896.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5879-5896
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 14
    • 33846561471 scopus 로고    scopus 로고
    • Practical aspects of (1)H transverse paramagnetic relaxation enhancement measurements on macromolecules
    • Iwahara, J., Tang, C., and Marius Clore, G. (2007). Practical aspects of (1)H transverse paramagnetic relaxation enhancement measurements on macromolecules. J. Magn. Reson. 184, 185-195.
    • (2007) J. Magn. Reson. , vol.184 , pp. 185-195
    • Iwahara, J.1    Tang, C.2    Marius Clore, G.3
  • 17
    • 0034717007 scopus 로고    scopus 로고
    • Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution
    • Kolbe, M., Besir, H., Essen, L.O., and Oesterhelt, D. (2000). Structure of the light-driven chloride pump halorhodopsin at 1.8 A resolution. Science 288, 1390-1396.
    • (2000) Science , vol.288 , pp. 1390-1396
    • Kolbe, M.1    Besir, H.2    Essen, L.O.3    Oesterhelt, D.4
  • 18
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14, 51-55, 29-32.
    • (1996) J. Mol. Graph. , vol.14
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 19
    • 0024853292 scopus 로고
    • Spin labeling of proteins
    • Kosen, P.A. (1989). Spin labeling of proteins. Methods Enzymol. 177, 86-121.
    • (1989) Methods Enzymol. , vol.177 , pp. 86-121
    • Kosen, P.A.1
  • 20
    • 36048971123 scopus 로고    scopus 로고
    • Structure of outer membrane protein G by solution NMR spectroscopy
    • Liang, B.Y., and Tamm, L.K. (2007). Structure of outer membrane protein G by solution NMR spectroscopy. Proc. Natl. Acad. Sci. USA 104, 16140-16145.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 16140-16145
    • Liang, B.Y.1    Tamm, L.K.2
  • 21
    • 33645472931 scopus 로고    scopus 로고
    • Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy
    • Liang, B.Y., Bushweller, J.H., and Tamm, L.K. (2006). Site-directed parallel spin-labeling and paramagnetic relaxation enhancement in structure determination of membrane proteins by solution NMR spectroscopy. J. Am. Chem. Soc. 128, 4389-4397.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4389-4397
    • Liang, B.Y.1    Bushweller, J.H.2    Tamm, L.K.3
  • 23
    • 58149475508 scopus 로고    scopus 로고
    • Backbone structure of a small helical integral membrane protein: A unique structural characterization
    • Page, R.C., Lee, S., Moore, J.D., Opella, S.J., and Cross, T.A. (2009). Backbone structure of a small helical integral membrane protein: a unique structural characterization. Protein Sci. 18, 134-146.
    • (2009) Protein Sci. , vol.18 , pp. 134-146
    • Page, R.C.1    Lee, S.2    Moore, J.D.3    Opella, S.J.4    Cross, T.A.5
  • 27
    • 57749192468 scopus 로고    scopus 로고
    • Solution state NMR structure and dynamics of KpOmpA, a 210 residue transmembrane domain possessing a high potential for immunological applications
    • Renault, M., Saurel, O., Czaplicki, J., Demange, P., Gervais, V., Löhr, F., Réat, V., Piotto, M., and 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.
    • (2009) J. Mol. Biol. , vol.385 , pp. 117-130
    • Renault, M.1    Saurel, O.2    Czaplicki, J.3    Demange, P.4    Gervais, V.5    Löhr, F.6    Réat, V.7    Piotto, M.8    Milon, A.9
  • 28
    • 14544292475 scopus 로고    scopus 로고
    • NMR structure of Mistic, a membrane-integrating protein for membrane protein expression
    • Roosild, T.P., Greenwald, J., Vega, M., Castronovo, S., Riek, R., and Choe, S. (2005). NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science 307, 1317-1321.
    • (2005) Science , vol.307 , pp. 1317-1321
    • Roosild, T.P.1    Greenwald, J.2    Vega, M.3    Castronovo, S.4    Riek, R.5    Choe, S.6
  • 29
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Shen, Y., Delaglio, F., Cornilescu, G., and Bax, A. (2009). TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J. Biomol. NMR 44, 213-223.
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 31
    • 0000825481 scopus 로고
    • A statistical method for evaluating systematic relationships
    • Sokal, R.R., and Michener, C.D. (1958). A statistical method for evaluating systematic relationships. University of Kansas Science Bulletin 38, 1409-1438.
    • (1958) University of Kansas Science Bulletin , vol.38 , pp. 1409-1438
    • Sokal, R.R.1    Michener, C.D.2
  • 32
    • 34250176566 scopus 로고    scopus 로고
    • Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles
    • Teriete, P., Franzin, C.M., Choi, J., and Marassi, F.M. (2007). Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles. Biochemistry 46, 6774-6783.
    • (2007) Biochemistry , vol.46 , pp. 6774-6783
    • Teriete, P.1    Franzin, C.M.2    Choi, J.3    Marassi, F.M.4
  • 33
    • 25844528201 scopus 로고    scopus 로고
    • Efficient strategy for the rapid backbone assignment of membrane proteins
    • Trbovic, N., Klammt, C., Koglin, A., Löhr, F., Bernhard, F., and Dötsch, V. (2005). Efficient strategy for the rapid backbone assignment of membrane proteins. J. Am. Chem. Soc. 127, 13504-13505.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13504-13505
    • Trbovic, N.1    Klammt, C.2    Koglin, A.3    Löhr, F.4    Bernhard, F.5    Dötsch, V.6
  • 34
    • 34547687784 scopus 로고    scopus 로고
    • Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy
    • Tugarinov, V., Kanelis, V., and Kay, L.E. (2006). Isotope labeling strategies for the study of high-molecular-weight proteins by solution NMR spectroscopy. Nat. Protoc. 1, 749-754.
    • (2006) Nat. Protoc. , vol.1 , pp. 749-754
    • Tugarinov, V.1    Kanelis, V.2    Kay, L.E.3
  • 36
    • 33750886311 scopus 로고    scopus 로고
    • Crystal structure of a rhomboid family intramembrane protease
    • Wang, Y.C., Zhang, Y.J., and Ha, Y. (2006). Crystal structure of a rhomboid family intramembrane protease. Nature 444, 179-180.
    • (2006) Nature , vol.444 , pp. 179-180
    • Wang, Y.C.1    Zhang, Y.J.2    Ha, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.