-
1
-
-
0031595590
-
15N multidimensional NMR to study the structure and dynamics of proteins
-
15N multidimensional NMR to study the structure and dynamics of proteins Annu. Rev. Biophys. Biomol. Struct. 27:1998;357-406.
-
(1998)
Annu. Rev. Biophys. Biomol. Struct.
, vol.27
, pp. 357-406
-
-
Gardner, K.H.1
Kay, L.E.2
-
2
-
-
0033038793
-
Improved segmental isotope labeling of proteins and application to a larger protein
-
Otomo T., Teruya K., Uegaki K., Yamazaki T., Kyogoku Y. Improved segmental isotope labeling of proteins and application to a larger protein. J. Biomol. NMR. 14:1999;105-114.
-
(1999)
J. Biomol. NMR
, vol.14
, pp. 105-114
-
-
Otomo, T.1
Teruya, K.2
Uegaki, K.3
Yamazaki, T.4
Kyogoku, Y.5
-
3
-
-
0033582287
-
Chemical ligation of folded recombinant proteins: Segmental isotopic labeling of domains for NMR studies
-
Xu R., Ayers B., Cowburn D., Muir T.W. Chemical ligation of folded recombinant proteins: segmental isotopic labeling of domains for NMR studies. Proc. Natl. Acad Sci. USA. 96:1999;388-393.
-
(1999)
Proc. Natl. Acad Sci. USA
, vol.96
, pp. 388-393
-
-
Xu, R.1
Ayers, B.2
Cowburn, D.3
Muir, T.W.4
-
4
-
-
0037077562
-
NMR study of 100 kDa HCV IRES RNA using segmental isotope labeling
-
Kim I., Lukavsky P.J., Puglisi J.D. NMR study of 100 kDa HCV IRES RNA using segmental isotope labeling. J. Am. Chem. Soc. 124:2002;9338-9339.
-
(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 9338-9339
-
-
Kim, I.1
Lukavsky, P.J.2
Puglisi, J.D.3
-
5
-
-
0030612833
-
2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
-
2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc. Natl. Acad Sci. USA. 94:1997;12366-12371.
-
(1997)
Proc. Natl. Acad Sci. USA
, vol.94
, pp. 12366-12371
-
-
Pervushin, K.1
Riek, R.2
Wider, G.3
Wüthrich, K.4
-
6
-
-
0037062977
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NMR analysis of a 900kDa GroEL-GroES complex
-
TROSY and CRINEPT NMR experiments are applied to the homoheptameric co-chaperonin GroES (72 kDa), either free in solution or in complex with the homotetradecameric chaperonin GroEL (800 kDa) or the single-ring GroEL variant SR1 (400 kDa). This paper establishes the use of TROSY and CRINEPT techniques for solution NMR studies of large macromolecular complexes up to 900 kDa, a size that has been generally considered to be inaccessible to analysis by solution NMR spectroscopy.
-
Fiaux J., Bertelsen E.B., Horwich A.L., Wüthrich K. NMR analysis of a 900kDa GroEL-GroES complex. Nature. 418:2002;207-211 TROSY and CRINEPT NMR experiments are applied to the homoheptameric co-chaperonin GroES (72 kDa), either free in solution or in complex with the homotetradecameric chaperonin GroEL (800 kDa) or the single-ring GroEL variant SR1 (400 kDa). This paper establishes the use of TROSY and CRINEPT techniques for solution NMR studies of large macromolecular complexes up to 900 kDa, a size that has been generally considered to be inaccessible to analysis by solution NMR spectroscopy.
-
(2002)
Nature
, vol.418
, pp. 207-211
-
-
Fiaux, J.1
Bertelsen, E.B.2
Horwich, A.L.3
Wüthrich, K.4
-
7
-
-
0037120882
-
Solution NMR techniques for large molecular and supramolecular structures
-
Riek R., Fiaux J., Bertelsen E.B., Horwich A.L., Wüthrich K. Solution NMR techniques for large molecular and supramolecular structures. J. Am. Chem. Soc. 124:2002;12144-12153.
-
(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 12144-12153
-
-
Riek, R.1
Fiaux, J.2
Bertelsen, E.B.3
Horwich, A.L.4
Wüthrich, K.5
-
9
-
-
0032506009
-
TROSY in triple-resonance experiments: New perspectives for sequential NMR assignment of large proteins
-
Salzmann M., Pervushin K., Wider G., Senn H., Wüthrich K. TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins. Proc. Natl. Acad Sci. USA. 95:1998;13585-13590.
-
(1998)
Proc. Natl. Acad Sci. USA
, vol.95
, pp. 13585-13590
-
-
Salzmann, M.1
Pervushin, K.2
Wider, G.3
Senn, H.4
Wüthrich, K.5
-
10
-
-
0033518575
-
TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins
-
Salzmann M., Wider G., Pervushin K., Senn H., Wüthrich K. TROSY-type triple-resonance experiments for sequential NMR assignments of large proteins. J. Am. Chem. Soc. 121:1999;844-848.
-
(1999)
J. Am. Chem. Soc.
, vol.121
, pp. 844-848
-
-
Salzmann, M.1
Wider, G.2
Pervushin, K.3
Senn, H.4
Wüthrich, K.5
-
11
-
-
0033599567
-
TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein
-
Yang D.W., Kay L.E. TROSY triple-resonance four-dimensional NMR spectroscopy of a 46 ns tumbling protein. J. Am. Chem. Soc. 121:1999;2571-2575.
-
(1999)
J. Am. Chem. Soc.
, vol.121
, pp. 2571-2575
-
-
Yang, D.W.1
Kay, L.E.2
-
14
-
-
0344994534
-
NMR spectroscopy of large molecules and multimolecular assemblies in solution
-
Wider G., Wüthrich K. NMR spectroscopy of large molecules and multimolecular assemblies in solution. Curr. Opin. Struct. Biol. 9:1999;594-601.
-
(1999)
Curr. Opin. Struct. Biol.
, vol.9
, pp. 594-601
-
-
Wider, G.1
Wüthrich, K.2
-
15
-
-
0033637980
-
Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology
-
A detailed review on TROSY, with a special emphasis on NMR experimentation and applications.
-
Pervushin K. Impact of transverse relaxation optimized spectroscopy (TROSY) on NMR as a technique in structural biology. Q. Rev. Biophys. 33:2000;161-197 A detailed review on TROSY, with a special emphasis on NMR experimentation and applications.
-
(2000)
Q. Rev. Biophys.
, vol.33
, pp. 161-197
-
-
Pervushin, K.1
-
16
-
-
0037045306
-
Current approaches for the study of large proteins by NMR
-
Venters R.A., Thompson R., Cavanagh J. Current approaches for the study of large proteins by NMR. J. Mol. Struct. 602:2002;275-292.
-
(2002)
J. Mol. Struct.
, vol.602
, pp. 275-292
-
-
Venters, R.A.1
Thompson, R.2
Cavanagh, J.3
-
17
-
-
0036509606
-
High-resolution nuclear magnetic resonance applied to biophysics and molecular biology: Highlights and challenges
-
Wider G. High-resolution nuclear magnetic resonance applied to biophysics and molecular biology: Highlights and challenges. IEEE T. Appl. Supercon. 12:2002;740-745.
-
(2002)
IEEE T. Appl. Supercon.
, vol.12
, pp. 740-745
-
-
Wider, G.1
-
18
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-
0031027910
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Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR
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Gardner K.H., Rosen M.K., Kay L.E. Global folds of highly deuterated, methyl-protonated proteins by multidimensional NMR. Biochemistry. 36:1997;1389-1401.
-
(1997)
Biochemistry
, vol.36
, pp. 1389-1401
-
-
Gardner, K.H.1
Rosen, M.K.2
Kay, L.E.3
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19
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0036700404
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Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles
-
Sequence-specific assignments were obtained for sidechain methyl resonances of valine, leucine and isoleucine in the integral membrane protein OmpX in 60 kDa micelles. The assignments are based on new TROSY-type NMR experiments combined with selective methyl group protonation on an otherwise deuterated background. The results increase the potential of solution NMR for de novo structure determination and for functional studies of large proteins.
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Hilty C., Fernández C., Wider G., Wüthrich K. Side chain NMR assignments in the membrane protein OmpX reconstituted in DHPC micelles. J. Biomol. NMR. 23:2002;289-301 Sequence-specific assignments were obtained for sidechain methyl resonances of valine, leucine and isoleucine in the integral membrane protein OmpX in 60 kDa micelles. The assignments are based on new TROSY-type NMR experiments combined with selective methyl group protonation on an otherwise deuterated background. The results increase the potential of solution NMR for de novo structure determination and for functional studies of large proteins.
-
(2002)
J. Biomol. NMR
, vol.23
, pp. 289-301
-
-
Hilty, C.1
Fernández, C.2
Wider, G.3
Wüthrich, K.4
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20
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0037189901
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Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase G
-
The authors report the largest single-chain protein (723 residues, 81 kDa) for which sequential resonance assignments have been obtained by solution NMR spectroscopy to date. Almost complete backbone assignments were achieved by the application of 4D TROSY-based NMR experiments, demonstrating that monomeric proteins of this size are accessible to structural and functional studies by solution NMR.
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Tugarinov V., Muhandiram R., Ayed A., Kay L.E. Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase G. J. Am. Chem. Soc. 124:2002;10025-10035 The authors report the largest single-chain protein (723 residues, 81 kDa) for which sequential resonance assignments have been obtained by solution NMR spectroscopy to date. Almost complete backbone assignments were achieved by the application of 4D TROSY-based NMR experiments, demonstrating that monomeric proteins of this size are accessible to structural and functional studies by solution NMR.
-
(2002)
J. Am. Chem. Soc.
, vol.124
, pp. 10025-10035
-
-
Tugarinov, V.1
Muhandiram, R.2
Ayed, A.3
Kay, L.E.4
-
21
-
-
0032036838
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Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis
-
Yabuki T., Kigawa T., Dohmae N., Takio K., Terada T., Ito Y., Laue E.D., Cooper J.A., Kainosho M., Yokoyama S. Dual amino acid-selective and site-directed stable-isotope labeling of the human c-Ha-Ras protein by cell-free synthesis. J. Biomol. NMR. 11:1998;295-306.
-
(1998)
J. Biomol. NMR
, vol.11
, pp. 295-306
-
-
Yabuki, T.1
Kigawa, T.2
Dohmae, N.3
Takio, K.4
Terada, T.5
Ito, Y.6
Laue, E.D.7
Cooper, J.A.8
Kainosho, M.9
Yokoyama, S.10
-
22
-
-
0032923295
-
Cell-free production and stable-isotope labeling of milligram quantities of proteins
-
Kigawa T., Yabuki T., Yoshida Y., Tsutsui M., Ito Y., Shibata T., Yokoyama S. Cell-free production and stable-isotope labeling of milligram quantities of proteins. FEBS Lett. 442:1999;15-19.
-
(1999)
FEBS Lett.
, vol.442
, pp. 15-19
-
-
Kigawa, T.1
Yabuki, T.2
Yoshida, Y.3
Tsutsui, M.4
Ito, Y.5
Shibata, T.6
Yokoyama, S.7
-
23
-
-
0037162453
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An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system
-
Kiga D., Sakamoto K., Kodama K., Kigawa T., Matsuda T., Yabuki T., Shirouzu M., Harada Y., Nakayama H., Takio K.et al. An engineered Escherichia coli tyrosyl-tRNA synthetase for site-specific incorporation of an unnatural amino acid into proteins in eukaryotic translation and its application in a wheat germ cell-free system. Proc. Natl. Acad. Sci. USA. 99:2002;9715-9720.
-
(2002)
Proc. Natl. Acad. Sci. USA
, vol.99
, pp. 9715-9720
-
-
Kiga, D.1
Sakamoto, K.2
Kodama, K.3
Kigawa, T.4
Matsuda, T.5
Yabuki, T.6
Shirouzu, M.7
Harada, Y.8
Nakayama, H.9
Takio, K.10
-
24
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0034625918
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NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments
-
TROSY triple-resonance experiments with aldolase, a symmetric homo-octameric protein of molecular mass 110 kDa, showed 20-50-fold sensitivity gains compared to the corresponding conventional NMR experiments. The authors demonstrate that sequence-specific assignments and identification of the regular secondary structures can be achieved for proteins in particles with a molecular mass beyond 100 kDa using TROSY NMR spectroscopy.
-
Salzmann M., Pervushin K., Wider G., Senn H., Wüthrich K. NMR assignment and secondary structure determination of an octameric 110 kDa protein using TROSY in triple resonance experiments. J. Am. Chem. Soc. 122:2000;7543-7548 TROSY triple-resonance experiments with aldolase, a symmetric homo-octameric protein of molecular mass 110 kDa, showed 20-50-fold sensitivity gains compared to the corresponding conventional NMR experiments. The authors demonstrate that sequence-specific assignments and identification of the regular secondary structures can be achieved for proteins in particles with a molecular mass beyond 100 kDa using TROSY NMR spectroscopy.
-
(2000)
J. Am. Chem. Soc.
, vol.122
, pp. 7543-7548
-
-
Salzmann, M.1
Pervushin, K.2
Wider, G.3
Senn, H.4
Wüthrich, K.5
-
25
-
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0036416144
-
TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility
-
McElroy C., Manfredo A., Wendt A., Gollnick P., Foster M. TROSY-NMR studies of the 91 kDa TRAP protein reveal allosteric control of a gene regulatory protein by ligand-altered flexibility. J. Mol. Biol. 323:2002;463-473.
-
(2002)
J. Mol. Biol.
, vol.323
, pp. 463-473
-
-
McElroy, C.1
Manfredo, A.2
Wendt, A.3
Gollnick, P.4
Foster, M.5
-
27
-
-
0033609011
-
Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules
-
Riek R., Wider G., Pervushin K., Wüthrich K. Polarization transfer by cross-correlated relaxation in solution NMR with very large molecules. Proc. Natl. Acad. Sci. USA. 96:1999;4918-4923.
-
(1999)
Proc. Natl. Acad. Sci. USA
, vol.96
, pp. 4918-4923
-
-
Riek, R.1
Wider, G.2
Pervushin, K.3
Wüthrich, K.4
-
28
-
-
0034170879
-
Protein dynamics measurements by TROSY-based NMR experiments
-
Zhu G., Xia Y.L., Nicholson L.K., Sze K.H. Protein dynamics measurements by TROSY-based NMR experiments. J. Magn. Reson. 143:2000;423-426.
-
(2000)
J. Magn. Reson.
, vol.143
, pp. 423-426
-
-
Zhu, G.1
Xia, Y.L.2
Nicholson, L.K.3
Sze, K.H.4
-
29
-
-
0036301762
-
Protein dynamics measurements by 3D HNCO based NMR experiments
-
Xia Y.L., Sze K.H., Li N., Shaw P.C., Zhu G. Protein dynamics measurements by 3D HNCO based NMR experiments. Spectrosc. Int. J. 16:2002;1-13.
-
(2002)
Spectrosc. Int. J.
, vol.16
, pp. 1-13
-
-
Xia, Y.L.1
Sze, K.H.2
Li, N.3
Shaw, P.C.4
Zhu, G.5
-
31
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0035956956
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Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles
-
This paper describes TROSY-based NMR studies of the integral membrane protein OmpX in 60 kDa DHPC micelles. It showed that TROSY methods can be used to obtain the 3D folds of integral membrane proteins in detergent micelles.
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Fernández C., Adeishvili K., Wüthrich K. Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles. Proc. Natl. Acad. Sci. USA. 98:2001;2358-2363 This paper describes TROSY-based NMR studies of the integral membrane protein OmpX in 60 kDa DHPC micelles. It showed that TROSY methods can be used to obtain the 3D folds of integral membrane proteins in detergent micelles.
-
(2001)
Proc. Natl. Acad. Sci. USA
, vol.98
, pp. 2358-2363
-
-
Fernández, C.1
Adeishvili, K.2
Wüthrich, K.3
-
32
-
-
0035979788
-
Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli
-
Fernández C., Hilty C., Bonjour S., Adeishvili K., Pervushin K., Wüthrich K. Solution NMR studies of the integral membrane proteins OmpX and OmpA from Escherichia coli. FEBS Lett. 504:2001;173-178.
-
(2001)
FEBS Lett.
, vol.504
, pp. 173-178
-
-
Fernández, C.1
Hilty, C.2
Bonjour, S.3
Adeishvili, K.4
Pervushin, K.5
Wüthrich, K.6
-
33
-
-
0035066331
-
Structure of outer membrane protein A transmembrane domain by NMR spectroscopy
-
This paper describes the 3D fold determination of the integral membrane protein OmpA in DPC micelles of 50 kDa. Dynamic studies by TROSY-type NMR experiments suggest that conformational flexibility in the structure may contribute to the membrane channel function of this protein.
-
Arora A., Abildgaard F., Bushweller J.H., Tamm L.K. Structure of outer membrane protein A transmembrane domain by NMR spectroscopy. Nat. Struct. Biol. 8:2001;334-338 This paper describes the 3D fold determination of the integral membrane protein OmpA in DPC micelles of 50 kDa. Dynamic studies by TROSY-type NMR experiments suggest that conformational flexibility in the structure may contribute to the membrane channel function of this protein.
-
(2001)
Nat. Struct. Biol.
, vol.8
, pp. 334-338
-
-
Arora, A.1
Abildgaard, F.2
Bushweller, J.H.3
Tamm, L.K.4
-
34
-
-
0035443197
-
Biophysical approaches to membrane protein structure determination
-
Arora A., Tamm L.K. Biophysical approaches to membrane protein structure determination. Curr. Opin. Struct. Biol. 11:2001;540-547.
-
(2001)
Curr. Opin. Struct. Biol.
, vol.11
, pp. 540-547
-
-
Arora, A.1
Tamm, L.K.2
-
35
-
-
0037108964
-
Solution structure and dynamics of the outer membrane enzyme PagP by NMR
-
This paper describes the determination by solution NMR of the 3D fold of the outer membrane enzyme PagP both in DPC and in n-octyl-β-D-glucoside micelles of size 50-60 kDa. The 3D solution fold of PagP provides a structural basis for the biological mechanism of action of this protein.
-
Hwang P.M., Choy W., Lo E.I., Chen L., Forman-Kay J.D., Raetz C.R.H., Privé G.G., Bishop R.E., Kay L.E. Solution structure and dynamics of the outer membrane enzyme PagP by NMR. Proc. Natl. Acad Sci. USA. 99:2002;13560-13565 This paper describes the determination by solution NMR of the 3D fold of the outer membrane enzyme PagP both in DPC and in n-octyl-β-D-glucoside micelles of size 50-60 kDa. The 3D solution fold of PagP provides a structural basis for the biological mechanism of action of this protein.
-
(2002)
Proc. Natl. Acad Sci. USA
, vol.99
, pp. 13560-13565
-
-
Hwang, P.M.1
Choy, W.2
Lo, E.I.3
Chen, L.4
Forman-Kay, J.D.5
Raetz, C.R.H.6
Privé, G.G.7
Bishop, R.E.8
Kay, L.E.9
-
36
-
-
0033932639
-
β-Barrel membrane proteins
-
Schulz G.E. β-Barrel membrane proteins. Curr. Opin. Struct. Biol. 10:2000;443-447.
-
(2000)
Curr. Opin. Struct. Biol.
, vol.10
, pp. 443-447
-
-
Schulz, G.E.1
-
37
-
-
0037020298
-
Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: Resonance assignment of native bacteriorhodopsin
-
Schubert M., Kolbe M., Kessler B., Oesterhelt D., Schmieder P. Heteronuclear multidimensional NMR spectroscopy of solubilized membrane proteins: Resonance assignment of native bacteriorhodopsin. Chembiochem. 3:2002;1019-1023.
-
(2002)
Chembiochem.
, vol.3
, pp. 1019-1023
-
-
Schubert, M.1
Kolbe, M.2
Kessler, B.3
Oesterhelt, D.4
Schmieder, P.5
-
38
-
-
0037159196
-
Topology and secondary structure of the N-terminal domain of diacylglycerol kinase
-
The authors describe the topology and secondary structure of the N-terminal domain of the membrane protein diacylglygerol kinase in DPC micelles, determined by TROSY-type NMR techniques.
-
Oxenoid K., Sonnichsen F.D., Sanders C.R. Topology and secondary structure of the N-terminal domain of diacylglycerol kinase. Biochemistry. 41:2002;12876-12882 The authors describe the topology and secondary structure of the N-terminal domain of the membrane protein diacylglygerol kinase in DPC micelles, determined by TROSY-type NMR techniques.
-
(2002)
Biochemistry
, vol.41
, pp. 12876-12882
-
-
Oxenoid, K.1
Sonnichsen, F.D.2
Sanders, C.R.3
-
40
-
-
0036490372
-
NMR in drug discovery
-
A detailed review on NMR applications in structure-based drug design. The principles that enable NMR to provide information on the nature of molecular interactions and current NMR-based strategies to identify lead compounds in drug discovery are surveyed.
-
Pellecchia M., Sem D.S., Wüthrich K. NMR in drug discovery. Nat. Rev. Drug Discov. 1:2002;211-219 A detailed review on NMR applications in structure-based drug design. The principles that enable NMR to provide information on the nature of molecular interactions and current NMR-based strategies to identify lead compounds in drug discovery are surveyed.
-
(2002)
Nat. Rev. Drug Discov.
, vol.1
, pp. 211-219
-
-
Pellecchia, M.1
Sem, D.S.2
Wüthrich, K.3
-
41
-
-
0032918076
-
Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR
-
Pellecchia M., Sebbel P., Hermanns U., Wüthrich K., Glockshuber R. Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR. Nat. Struct. Biol. 6:1999;336-339.
-
(1999)
Nat. Struct. Biol.
, vol.6
, pp. 336-339
-
-
Pellecchia, M.1
Sebbel, P.2
Hermanns, U.3
Wüthrich, K.4
Glockshuber, R.5
-
42
-
-
0035184240
-
Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe
-
Gronwald W., Huber F., Grunewald P., Sporner M., Wohlgemuth S., Herrmann C., Kalbitzer H.R. Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe. Structure. 9:2001;1029-1041.
-
(2001)
Structure
, vol.9
, pp. 1029-1041
-
-
Gronwald, W.1
Huber, F.2
Grunewald, P.3
Sporner, M.4
Wohlgemuth, S.5
Herrmann, C.6
Kalbitzer, H.R.7
-
43
-
-
0037204076
-
Three-dimensional structure of the complexin/SNARE complex
-
Chen X.C., Tomchick D.R., Kovrigin E., Arac D., Machius M., Sudhof T.C., Rizo J. Three-dimensional structure of the complexin/SNARE complex. Neuron. 33:2002;397-409.
-
(2002)
Neuron
, vol.33
, pp. 397-409
-
-
Chen, X.C.1
Tomchick, D.R.2
Kovrigin, E.3
Arac, D.4
Machius, M.5
Sudhof, T.C.6
Rizo, J.7
-
44
-
-
0037133347
-
TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain
-
Frickel E.M., Riek R., Jelesarov I., Helenius A., Wüthrich K., Ellgaard L. TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain. Proc. Natl. Acad Sci. USA. 99:2002;1954-1959.
-
(2002)
Proc. Natl. Acad Sci. USA
, vol.99
, pp. 1954-1959
-
-
Frickel, E.M.1
Riek, R.2
Jelesarov, I.3
Helenius, A.4
Wüthrich, K.5
Ellgaard, L.6
-
45
-
-
0037143625
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CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90
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Rudiger S., Freund S.M.V., Veprintsev D.B., Fersht A.R. CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90. Proc. Natl. Acad Sci. USA. 99:2002;11085-11090.
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(2002)
Proc. Natl. Acad Sci. USA
, vol.99
, pp. 11085-11090
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Rudiger, S.1
Freund, S.M.V.2
Veprintsev, D.B.3
Fersht, A.R.4
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46
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0034051065
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A novel NMR method for determining the interfaces of large protein-protein complexes
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A novel NMR method to determine the interfaces of large complexes is described and applied to a 64 kDa complex. The experiment uses saturation phenomena in combination with TROSY in a deuterium-labeled system.
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Takahashi H., Nakanishi T., Kami K., Arata Y., Shimada I. A novel NMR method for determining the interfaces of large protein-protein complexes. Nat. Struct. Biol. 7:2000;220-223 A novel NMR method to determine the interfaces of large complexes is described and applied to a 64 kDa complex. The experiment uses saturation phenomena in combination with TROSY in a deuterium-labeled system.
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(2000)
Nat. Struct. Biol.
, vol.7
, pp. 220-223
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Takahashi, H.1
Nakanishi, T.2
Kami, K.3
Arata, Y.4
Shimada, I.5
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47
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0034809894
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SEA-TROSY (solvent exposed amides with TROSY): A method to resolve the problem of spectral overlap in very large proteins
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Pellecchia M., Meininger D., Shen A.L., Jack R., Kasper C.B., Sem D.S. SEA-TROSY (solvent exposed amides with TROSY): a method to resolve the problem of spectral overlap in very large proteins. J. Am. Chem. Soc. 123:2001;4633-4634.
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(2001)
J. Am. Chem. Soc.
, vol.123
, pp. 4633-4634
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Pellecchia, M.1
Meininger, D.2
Shen, A.L.3
Jack, R.4
Kasper, C.B.5
Sem, D.S.6
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49
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0032564349
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NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation optimized spectroscopy
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Pervushin K., Ono A., Fernández C., Szyperski T., Kainosho M., Wüthrich K. NMR scalar couplings across Watson-Crick base pair hydrogen bonds in DNA observed by transverse relaxation optimized spectroscopy. Proc. Natl. Acad. Sci. USA. 95:1998;14147-14151.
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(1998)
Proc. Natl. Acad. Sci. USA
, vol.95
, pp. 14147-14151
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Pervushin, K.1
Ono, A.2
Fernández, C.3
Szyperski, T.4
Kainosho, M.5
Wüthrich, K.6
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51
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0033621766
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HN coupling constants across Watson-Crick base pairs in the Antennapedia homeodomain-DNA complex using TROSY
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This paper describes NMR measurements of scalar couplings across hydrogen bonds in Watson-Crick base pairs in a 17 kDa Antennapedia homeodomain-DNA complex. Measurement of these couplings enables comparative studies of nucleic acid structure free in solution and in complexes.
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HN coupling constants across Watson-Crick base pairs in the Antennapedia homeodomain-DNA complex using TROSY J. Biomol. NMR. 16:2000;39-46 This paper describes NMR measurements of scalar couplings across hydrogen bonds in Watson-Crick base pairs in a 17 kDa Antennapedia homeodomain-DNA complex. Measurement of these couplings enables comparative studies of nucleic acid structure free in solution and in complexes.
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(2000)
J. Biomol. NMR
, vol.16
, pp. 39-46
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Pervushin, K.1
Fernández, C.2
Riek, R.3
Ono, A.4
Kainosho, M.5
Wüthrich, K.6
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53
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0032586932
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NC′ connectivities across hydrogen bonds in a 30 kDa protein
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NC′ connectivities across hydrogen bonds in a 30 kDa protein J. Biomol. NMR. 14:1999;181-184.
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(1999)
J. Biomol. NMR
, vol.14
, pp. 181-184
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Wang, Y.X.1
Jacob, J.2
Cordier, F.3
Wingfield, P.4
Stahl, S.J.5
Lee-Huang, S.6
Torchia, D.7
Grzesiek, S.8
Bax, A.9
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54
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0040518458
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Detection of scalar couplings across NḢOP and OḢOP hydrogen bonds in a flavoprotein
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Löhr F., Mayhew S.G., Ruterjans H. Detection of scalar couplings across. NḢOP and OḢOP hydrogen bonds in a flavoprotein J. Am. Chem. Soc. 122:2000;9289-9295.
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(2000)
J. Am. Chem. Soc.
, vol.122
, pp. 9289-9295
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Löhr, F.1
Mayhew, S.G.2
Ruterjans, H.3
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55
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0037022781
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Direct detection of hydrogen bonds in monomeric superoxide dismutase: Biological implications
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Banci L., Felli I.C., Kummerle R. Direct detection of hydrogen bonds in monomeric superoxide dismutase: biological implications. Biochemistry. 41:2002;2913-2920.
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(2002)
Biochemistry
, vol.41
, pp. 2913-2920
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Banci, L.1
Felli, I.C.2
Kummerle, R.3
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56
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0036756444
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Direct NMR observation and DFT calculations of a hydrogen bond at the active site of a 44 kDa enzyme
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The authors describe the observation of a hydrogen bond in the active site of a 44 kDa trimeric enzyme using improved TROSY-based NMR techniques. The presence of this hydrogen bond was demonstrated by the measurement of trans hydrogen-bond couplings and by the transfer of polarization across the hydrogen bond. This technique provides unique information about the enzyme and its complexes, which is very useful for structural refinement of atomic models.
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Eletsky A., Heinz T., Moreira O., Kienhofer A., Hilvert D., Pervushin K. Direct NMR observation and DFT calculations of a hydrogen bond at the active site of a 44 kDa enzyme. J. Biomol. NMR. 24:2002;31-39 The authors describe the observation of a hydrogen bond in the active site of a 44 kDa trimeric enzyme using improved TROSY-based NMR techniques. The presence of this hydrogen bond was demonstrated by the measurement of trans hydrogen-bond couplings and by the transfer of polarization across the hydrogen bond. This technique provides unique information about the enzyme and its complexes, which is very useful for structural refinement of atomic models.
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(2002)
J. Biomol. NMR
, vol.24
, pp. 31-39
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Eletsky, A.1
Heinz, T.2
Moreira, O.3
Kienhofer, A.4
Hilvert, D.5
Pervushin, K.6
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60
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0034072742
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NMR solution structure determination of RNAs
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Mollova E.T., Pardi A. NMR solution structure determination of RNAs. Curr. Opin. Struct. Biol. 10:2000;298-302.
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(2000)
Curr. Opin. Struct. Biol.
, vol.10
, pp. 298-302
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Mollova, E.T.1
Pardi, A.2
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61
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0035689920
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Transverse relaxation optimized HCN experiment for nucleic acids: Combining the advantages of TROSY and MQ spin evolution
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Brutscher B., Simorre J.P. Transverse relaxation optimized HCN experiment for nucleic acids: Combining the advantages of TROSY and MQ spin evolution. J. Biomol. NMR. 21:2001;367-372.
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(2001)
J. Biomol. NMR
, vol.21
, pp. 367-372
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Brutscher, B.1
Simorre, J.P.2
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63
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0034073418
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Transverse relaxation optimized triple-resonance NMR experiments for nucleic acids
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Fiala R., Czernek J., Šklenar V. Transverse relaxation optimized triple-resonance NMR experiments for nucleic acids. J. Biomol. NMR. 16:2000;291-302.
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(2000)
J. Biomol. NMR
, vol.16
, pp. 291-302
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Fiala, R.1
Czernek, J.2
Šklenar, V.3
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