메뉴 건너뛰기




Volumn 23, Issue 5, 2013, Pages 734-739

NMR methods for structural studies of large monomeric and multimeric proteins

Author keywords

[No Author keywords available]

Indexed keywords

MONOMER; POLYMER;

EID: 84885833311     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2013.06.016     Document Type: Review
Times cited : (62)

References (61)
  • 1
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 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
    • Pervushin K., Riek R., Wider G., Wuthrich K. Attenuated T2 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 U S A 1997, 94:12366-12371.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 2
    • 0041930989 scopus 로고    scopus 로고
    • 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes
    • 13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes. J Am Chem Soc 2003, 125:10420-10428.
    • (2003) J Am Chem Soc , vol.125 , pp. 10420-10428
    • Tugarinov, V.1    Hwang, P.M.2    Ollerenshaw, J.E.3    Kay, L.E.4
  • 3
    • 4243114694 scopus 로고    scopus 로고
    • Resolution and sensitivity of high field nuclear magnetic resonance spectroscopy
    • Rovnyak D., Hoch J.C., Stern A.S., Wagner G. Resolution and sensitivity of high field nuclear magnetic resonance spectroscopy. J Biomol NMR 2004, 30:1-10.
    • (2004) J Biomol NMR , vol.30 , pp. 1-10
    • Rovnyak, D.1    Hoch, J.C.2    Stern, A.S.3    Wagner, G.4
  • 4
    • 67650082785 scopus 로고    scopus 로고
    • Recent advances in solution NMR: fast methods and heteronuclear direct detection
    • Isabella C., Felli B.B. Recent advances in solution NMR: fast methods and heteronuclear direct detection. ChemPhysChem 2009, 9999.
    • (2009) ChemPhysChem , vol.9999
    • Isabella, C.1    Felli, B.B.2
  • 5
    • 0003007299 scopus 로고
    • Exponential sampling, an alternative method for sampling in two-dimensional NMR experiments
    • Barna J.C.J., Laue E.D., Mayger M.R., Skilling J., Worrall S.J.P. Exponential sampling, an alternative method for sampling in two-dimensional NMR experiments. J Magn Reson 1987, 73:69-77.
    • (1987) J Magn Reson , vol.73 , pp. 69-77
    • Barna, J.C.J.1    Laue, E.D.2    Mayger, M.R.3    Skilling, J.4    Worrall, S.J.P.5
  • 6
    • 27644584200 scopus 로고    scopus 로고
    • Optimization of resolution and sensitivity of 4D NOESY using multi-dimensional decomposition
    • Luan T., Jaravine V., Yee A., Arrowsmith C.H., Orekhov V.Y. Optimization of resolution and sensitivity of 4D NOESY using multi-dimensional decomposition. J Biomol NMR 2005, 33:1-14.
    • (2005) J Biomol NMR , vol.33 , pp. 1-14
    • Luan, T.1    Jaravine, V.2    Yee, A.3    Arrowsmith, C.H.4    Orekhov, V.Y.5
  • 7
    • 4243138246 scopus 로고    scopus 로고
    • Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction
    • Rovnyak D., Frueh D.P., Sastry M., Sun Z.Y., Stern A.S., Hoch J.C., Wagner G. Accelerated acquisition of high resolution triple-resonance spectra using non-uniform sampling and maximum entropy reconstruction. J Magn Reson 2004, 170:15-21.
    • (2004) J Magn Reson , vol.170 , pp. 15-21
    • Rovnyak, D.1    Frueh, D.P.2    Sastry, M.3    Sun, Z.Y.4    Stern, A.S.5    Hoch, J.C.6    Wagner, G.7
  • 8
    • 70350303834 scopus 로고    scopus 로고
    • FM reconstruction of non-uniformly sampled protein NMR data at higher dimensions and optimization by distillation
    • Hyberts S.G., Frueh D.P., Arthanari H., Wagner G. FM reconstruction of non-uniformly sampled protein NMR data at higher dimensions and optimization by distillation. J Biomol NMR 2009, 45:283-294.
    • (2009) J Biomol NMR , vol.45 , pp. 283-294
    • Hyberts, S.G.1    Frueh, D.P.2    Arthanari, H.3    Wagner, G.4
  • 9
    • 35248859308 scopus 로고    scopus 로고
    • NMR data processing using iterative thresholding and minimum l(1)-norm reconstruction
    • Stern A.S., Donoho D.L., Hoch J.C. NMR data processing using iterative thresholding and minimum l(1)-norm reconstruction. J Magn Reson 2007, 188:295-300.
    • (2007) J Magn Reson , vol.188 , pp. 295-300
    • Stern, A.S.1    Donoho, D.L.2    Hoch, J.C.3
  • 10
    • 84865638176 scopus 로고    scopus 로고
    • Applications of non-uniform sampling and processing
    • Springer, Berlin/Heidelberg
    • Hyberts S., Arthanari H., Wagner G. Applications of non-uniform sampling and processing. Topics in Current Chemistry 2011, Springer, Berlin/Heidelberg, 1-24.
    • (2011) Topics in Current Chemistry , pp. 1-24
    • Hyberts, S.1    Arthanari, H.2    Wagner, G.3
  • 11
    • 84863114255 scopus 로고    scopus 로고
    • Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling
    • Hyberts S.G., Milbradt A.G., Wagner A.B., Arthanari H., Wagner G. Application of iterative soft thresholding for fast reconstruction of NMR data non-uniformly sampled with multidimensional Poisson Gap scheduling. J Biomol NMR 2012, 52:315-327.
    • (2012) J Biomol NMR , vol.52 , pp. 315-327
    • Hyberts, S.G.1    Milbradt, A.G.2    Wagner, A.B.3    Arthanari, H.4    Wagner, G.5
  • 12
    • 79959974154 scopus 로고    scopus 로고
    • Fast multidimensional NMR spectroscopy using compressed sensing
    • Holland D.J., Bostock M.J., Gladden L.F., Nietlispach D. Fast multidimensional NMR spectroscopy using compressed sensing. Angew Chem 2011, 50:6548-6551.
    • (2011) Angew Chem , vol.50 , pp. 6548-6551
    • Holland, D.J.1    Bostock, M.J.2    Gladden, L.F.3    Nietlispach, D.4
  • 13
    • 79958040716 scopus 로고    scopus 로고
    • Accelerated NMR spectroscopy by using compressed sensing
    • Kazimierczuk K., Orekhov V.Y. Accelerated NMR spectroscopy by using compressed sensing. Angew Chem 2011, 50:5556-5559.
    • (2011) Angew Chem , vol.50 , pp. 5556-5559
    • Kazimierczuk, K.1    Orekhov, V.Y.2
  • 14
    • 70349102122 scopus 로고    scopus 로고
    • A double TROSY hNCAnH experiment for efficient assignment of large and challenging proteins
    • Frueh D.P., Arthanari H., Koglin A., Walsh C.T., Wagner G. A double TROSY hNCAnH experiment for efficient assignment of large and challenging proteins. J Am Chem Soc 2009, 131:12880-12881.
    • (2009) J Am Chem Soc , vol.131 , pp. 12880-12881
    • Frueh, D.P.1    Arthanari, H.2    Koglin, A.3    Walsh, C.T.4    Wagner, G.5
  • 15
    • 84879552273 scopus 로고    scopus 로고
    • Exploring signal-to-noise ratio and sensitivity in non-uniformly sampled multi-dimensional NMR spectra
    • Hyberts S.G., Robson S.A., Wagner G. Exploring signal-to-noise ratio and sensitivity in non-uniformly sampled multi-dimensional NMR spectra. J Biomol NMR 2013, 55:167-178.
    • (2013) J Biomol NMR , vol.55 , pp. 167-178
    • Hyberts, S.G.1    Robson, S.A.2    Wagner, G.3
  • 16
    • 3943074512 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins
    • Tugarinov V., Hwang P.M., Kay L.E. Nuclear magnetic resonance spectroscopy of high-molecular-weight proteins. Annu Rev Biochem 2004, 73:107-146.
    • (2004) Annu Rev Biochem , vol.73 , pp. 107-146
    • Tugarinov, V.1    Hwang, P.M.2    Kay, L.E.3
  • 17
    • 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., Bax A. TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 2009, 44:213-223.
    • (2009) J Biomol NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 20
    • 68049084585 scopus 로고    scopus 로고
    • Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments
    • Liu Y., Prestegard J.H. Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments. J Magn Reson 2009, 200:109-118.
    • (2009) J Magn Reson , vol.200 , pp. 109-118
    • Liu, Y.1    Prestegard, J.H.2
  • 22
    • 34249023900 scopus 로고    scopus 로고
    • 13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy
    • 13C-methyl-group-labeled methionine precursor as a useful tool for simplifying protein structural analysis by NMR spectroscopy. ChemBioChem 2007, 8:610-612.
    • (2007) ChemBioChem , vol.8 , pp. 610-612
    • Fischer, M.1    Kloiber, K.2    Häusler, J.3    Ledolter, K.4    Konrat, R.5    Schmid, W.6
  • 23
    • 84859406875 scopus 로고    scopus 로고
    • Methionine scanning as an NMR tool for detecting and analyzing biomolecular interaction surfaces
    • Stoffregen Mira C., Schwer Matthias M., Renschler Fabian A., Wiesner S. Methionine scanning as an NMR tool for detecting and analyzing biomolecular interaction surfaces. Structure 2012, 20:573-581.
    • (2012) Structure , vol.20 , pp. 573-581
    • Stoffregen Mira, C.1    Schwer Matthias, M.2    Renschler Fabian, A.3    Wiesner, S.4
  • 26
    • 37849041010 scopus 로고    scopus 로고
    • A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues
    • Isaacson R.L., Simpson P.J., Liu M., Cota E., Zhang X., Freemont P., Matthews S. A new labeling method for methyl transverse relaxation-optimized spectroscopy NMR spectra of alanine residues. J Am Chem Soc 2007, 129:15428-15429.
    • (2007) J Am Chem Soc , vol.129 , pp. 15428-15429
    • Isaacson, R.L.1    Simpson, P.J.2    Liu, M.3    Cota, E.4    Zhang, X.5    Freemont, P.6    Matthews, S.7
  • 27
    • 58149463865 scopus 로고    scopus 로고
    • An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein
    • Ayala I., Sounier R., Usé N., Gans P., Boisbouvier J. An efficient protocol for the complete incorporation of methyl-protonated alanine in perdeuterated protein. J Biomol NMR 2009, 43:111-119.
    • (2009) J Biomol NMR , vol.43 , pp. 111-119
    • Ayala, I.1    Sounier, R.2    Usé, N.3    Gans, P.4    Boisbouvier, J.5
  • 28
    • 78149412689 scopus 로고    scopus 로고
    • A simple strategy for (1)(3)C, (1)H labeling at the Ile-gamma2 methyl position in highly deuterated proteins
    • Ruschak A.M., Velyvis A., Kay L.E. A simple strategy for (1)(3)C, (1)H labeling at the Ile-gamma2 methyl position in highly deuterated proteins. J Biomol NMR 2010, 48:129-135.
    • (2010) J Biomol NMR , vol.48 , pp. 129-135
    • Ruschak, A.M.1    Velyvis, A.2    Kay, L.E.3
  • 29
    • 80054984345 scopus 로고    scopus 로고
    • Hydrogen exchange study on the hydroxyl groups of serine and threonine residues in proteins and structure refinement using NOE restraints with polar side-chain groups
    • Takeda M., Jee J., Ono A.M., Terauchi T., Kainosho M. Hydrogen exchange study on the hydroxyl groups of serine and threonine residues in proteins and structure refinement using NOE restraints with polar side-chain groups. J Am Chem Soc 2011, 133:17420-17427.
    • (2011) J Am Chem Soc , vol.133 , pp. 17420-17427
    • Takeda, M.1    Jee, J.2    Ono, A.M.3    Terauchi, T.4    Kainosho, M.5
  • 30
    • 81855190757 scopus 로고    scopus 로고
    • Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes
    • Sinha K., Jen-Jacobson L., Rule G.S. Specific labeling of threonine methyl groups for NMR studies of protein-nucleic acid complexes. Biochemistry 2011, 50:10189-10191.
    • (2011) Biochemistry , vol.50 , pp. 10189-10191
    • Sinha, K.1    Jen-Jacobson, L.2    Rule, G.S.3
  • 31
    • 84866272306 scopus 로고    scopus 로고
    • 3-threonine for solution NMR studies of large protein complexes: application to the 670kDa proteasome
    • 3-threonine for solution NMR studies of large protein complexes: application to the 670kDa proteasome. PLoS ONE 2012, 7:e43725.
    • (2012) PLoS ONE , vol.7
    • Velyvis, A.1    Ruschak, A.M.2    Kay, L.E.3
  • 32
    • 63449103439 scopus 로고    scopus 로고
    • Methyl-detected 'out-and-back' NMR experiments for simultaneous assignments of Alaβ and Ileγ2 methyl groups in large proteins
    • Sheppard D., Guo C., Tugarinov V. Methyl-detected 'out-and-back' NMR experiments for simultaneous assignments of Alaβ and Ileγ2 methyl groups in large proteins. J Biomol NMR 2009, 43:229-238.
    • (2009) J Biomol NMR , vol.43 , pp. 229-238
    • Sheppard, D.1    Guo, C.2    Tugarinov, V.3
  • 33
    • 0000195125 scopus 로고
    • 15N]-HMQC, a pseudo-triple resonance experiment
    • 15N]-HMQC, a pseudo-triple resonance experiment. J Magn Reson 1991, 93:635-641.
    • (1991) J Magn Reson , vol.93 , pp. 635-641
    • Farmer, I.I.B.1
  • 35
    • 57549109459 scopus 로고    scopus 로고
    • Identification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection
    • Guo C., Tugarinov V. Identification of HN-methyl NOEs in large proteins using simultaneous amide-methyl TROSY-based detection. J Biomol NMR 2009, 43:21-30.
    • (2009) J Biomol NMR , vol.43 , pp. 21-30
    • Guo, C.1    Tugarinov, V.2
  • 36
    • 70350302655 scopus 로고    scopus 로고
    • Time-shared HSQC-NOESY for accurate distance constraints measured at high-field in (15)N-(13)C-ILV methyl labeled proteins
    • Frueh D.P., Leed A., Arthanari H., Koglin A., Walsh C.T., Wagner G. Time-shared HSQC-NOESY for accurate distance constraints measured at high-field in (15)N-(13)C-ILV methyl labeled proteins. J Biomol NMR 2009, 45:311-318.
    • (2009) J Biomol NMR , vol.45 , pp. 311-318
    • Frueh, D.P.1    Leed, A.2    Arthanari, H.3    Koglin, A.4    Walsh, C.T.5    Wagner, G.6
  • 37
    • 34548495116 scopus 로고    scopus 로고
    • Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping
    • Wurtz P., Aitio O., Hellman M., Permi P. Simultaneous detection of amide and methyl correlations using a time shared NMR experiment: application to binding epitope mapping. J Biomol NMR 2007, 39:97-105.
    • (2007) J Biomol NMR , vol.39 , pp. 97-105
    • Wurtz, P.1    Aitio, O.2    Hellman, M.3    Permi, P.4
  • 38
    • 33644531581 scopus 로고    scopus 로고
    • Determination of all nOes in 1H-13C-Me-ILV-U-2H-15N proteins with two time-shared experiments
    • Frueh D.P., Vosburg D.A., Walsh C.T., Wagner G. Determination of all nOes in 1H-13C-Me-ILV-U-2H-15N proteins with two time-shared experiments. J Biomol NMR 2006, 34:31-40.
    • (2006) J Biomol NMR , vol.34 , pp. 31-40
    • Frueh, D.P.1    Vosburg, D.A.2    Walsh, C.T.3    Wagner, G.4
  • 40
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • Sprangers R., Kay L.E. Quantitative dynamics and binding studies of the 20S proteasome by NMR. Nature 2007, 445:618-622.
    • (2007) Nature , vol.445 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 41
    • 77957970501 scopus 로고    scopus 로고
    • The proteasome antechamber maintains substrates in an unfolded state
    • Ruschak A.M., Religa T.L., Breuer S., Witt S., Kay L.E. The proteasome antechamber maintains substrates in an unfolded state. Nature 2010, 467:868-871.
    • (2010) Nature , vol.467 , pp. 868-871
    • Ruschak, A.M.1    Religa, T.L.2    Breuer, S.3    Witt, S.4    Kay, L.E.5
  • 42
    • 79851510775 scopus 로고    scopus 로고
    • Structural NMR of protein oligomers using hybrid methods
    • Wang X., Lee H-W., Liu Y., Prestegard J.H. Structural NMR of protein oligomers using hybrid methods. J Struct Biol 2011, 173:515-529.
    • (2011) J Struct Biol , vol.173 , pp. 515-529
    • Wang, X.1    Lee, H.-W.2    Liu, Y.3    Prestegard, J.H.4
  • 43
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • Zuiderweg E.R. Mapping protein-protein interactions in solution by NMR spectroscopy. Biochemistry 2002, 41:1-7.
    • (2002) Biochemistry , vol.41 , pp. 1-7
    • Zuiderweg, E.R.1
  • 44
    • 0036302354 scopus 로고    scopus 로고
    • Determination of the interface of a large protein complex by transferred cross-saturation measurements
    • Nakanishi T., Miyazawa M., Sakakura M., Terasawa H., Takahashi H., Shimada I. Determination of the interface of a large protein complex by transferred cross-saturation measurements. J Mol Biol 2002, 318:245-249.
    • (2002) J Mol Biol , vol.318 , pp. 245-249
    • Nakanishi, T.1    Miyazawa, M.2    Sakakura, M.3    Terasawa, H.4    Takahashi, H.5    Shimada, I.6
  • 45
    • 70349093561 scopus 로고    scopus 로고
    • Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes
    • Clore G.M., Iwahara J. Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes. Chem Rev 2009, 109:4108-4139.
    • (2009) Chem Rev , vol.109 , pp. 4108-4139
    • Clore, G.M.1    Iwahara, J.2
  • 46
    • 0029050883 scopus 로고
    • Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution
    • Tolman J.R., Flanagan J.M., Kennedy M.A., Prestegard J.H. Nuclear magnetic dipole interactions in field-oriented proteins: information for structure determination in solution. Proc Natl Acad Sci U S A 1995, 92:9279-9283.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9279-9283
    • Tolman, J.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 47
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra N., Bax A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 1997, 278:1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 48
    • 0033551495 scopus 로고    scopus 로고
    • Domain orientation and dynamics in multidomain proteins from residual dipolar couplings
    • Fischer M.W., Losonczi J.A., Weaver J.L., Prestegard J.H. Domain orientation and dynamics in multidomain proteins from residual dipolar couplings. Biochemistry 1999, 38:9013-9022.
    • (1999) Biochemistry , vol.38 , pp. 9013-9022
    • Fischer, M.W.1    Losonczi, J.A.2    Weaver, J.L.3    Prestegard, J.H.4
  • 49
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Bruschweiler R., Liao X., Wright P.E. Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science 1995, 268:886-889.
    • (1995) Science , vol.268 , pp. 886-889
    • Bruschweiler, R.1    Liao, X.2    Wright, P.E.3
  • 50
    • 2942544364 scopus 로고    scopus 로고
    • Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements
    • Fushman D., Varadan R., Assfalg M., Walker O. Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements. Prog NMR Spectrosc 2004, 44:189-214.
    • (2004) Prog NMR Spectrosc , vol.44 , pp. 189-214
    • Fushman, D.1    Varadan, R.2    Assfalg, M.3    Walker, O.4
  • 51
    • 77951972141 scopus 로고    scopus 로고
    • Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2
    • Chen X., Lee B.H., Finley D., Walters K.J. Structure of proteasome ubiquitin receptor hRpn13 and its activation by the scaffolding protein hRpn2. Mol Cell 2010, 38:404-415.
    • (2010) Mol Cell , vol.38 , pp. 404-415
    • Chen, X.1    Lee, B.H.2    Finley, D.3    Walters, K.J.4
  • 53
    • 77955273066 scopus 로고    scopus 로고
    • Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1
    • Leeper T.C., Qu X., Lu C., Moore C., Varani G. Novel protein-protein contacts facilitate mRNA 3'-processing signal recognition by Rna15 and Hrp1. J Mol Biol 2010, 401:334-349.
    • (2010) J Mol Biol , vol.401 , pp. 334-349
    • Leeper, T.C.1    Qu, X.2    Lu, C.3    Moore, C.4    Varani, G.5
  • 54
    • 79851509793 scopus 로고    scopus 로고
    • NMR and small-angle scattering-based structural analysis of protein complexes in solution
    • Madl T., Gabel F., Sattler M. NMR and small-angle scattering-based structural analysis of protein complexes in solution. J Struct Biol 2011, 173:472-482.
    • (2011) J Struct Biol , vol.173 , pp. 472-482
    • Madl, T.1    Gabel, F.2    Sattler, M.3
  • 55
    • 84883598626 scopus 로고    scopus 로고
    • Structure and dynamics of ribosomal protein L12: an ensemble model based on SAXS and NMR relaxation
    • Bernado P., Modig K., Grela P., Svergun D.I., Tchorzewski M., Pons M., Akke M. Structure and dynamics of ribosomal protein L12: an ensemble model based on SAXS and NMR relaxation. Biophys J 2010, 98:2374-2382.
    • (2010) Biophys J , vol.98 , pp. 2374-2382
    • Bernado, P.1    Modig, K.2    Grela, P.3    Svergun, D.I.4    Tchorzewski, M.5    Pons, M.6    Akke, M.7
  • 56
    • 77956641793 scopus 로고    scopus 로고
    • Solution structure of the 128kDa enzyme I dimer from Escherichia coli and its 146kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering
    • Schwieters C.D., Suh J.Y., Grishaev A., Ghirlando R., Takayama Y., Clore G.M. Solution structure of the 128kDa enzyme I dimer from Escherichia coli and its 146kDa complex with HPr using residual dipolar couplings and small- and wide-angle X-ray scattering. J Am Chem Soc 2010, 132:13026-13045.
    • (2010) J Am Chem Soc , vol.132 , pp. 13026-13045
    • Schwieters, C.D.1    Suh, J.Y.2    Grishaev, A.3    Ghirlando, R.4    Takayama, Y.5    Clore, G.M.6
  • 57
    • 79951659237 scopus 로고    scopus 로고
    • Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex
    • Dancheck B., Ragusa M.J., Allaire M., Nairn A.C., Page R., Peti W. Molecular investigations of the structure and function of the protein phosphatase 1-spinophilin-inhibitor 2 heterotrimeric complex. Biochemistry 2011, 50:1238-1246.
    • (2011) Biochemistry , vol.50 , pp. 1238-1246
    • Dancheck, B.1    Ragusa, M.J.2    Allaire, M.3    Nairn, A.C.4    Page, R.5    Peti, W.6
  • 58
    • 77951631601 scopus 로고    scopus 로고
    • Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase
    • Mittag T., Marsh J., Grishaev A., Orlicky S., Lin H., Sicheri F., Tyers M., Forman-Kay J.D. Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase. Structure 2010, 18:494-506.
    • (2010) Structure , vol.18 , pp. 494-506
    • Mittag, T.1    Marsh, J.2    Grishaev, A.3    Orlicky, S.4    Lin, H.5    Sicheri, F.6    Tyers, M.7    Forman-Kay, J.D.8
  • 60
    • 33744529377 scopus 로고    scopus 로고
    • Protein ligation: an enabling technology for the biophysical analysis of proteins
    • Muralidharan V., Muir T.W. Protein ligation: an enabling technology for the biophysical analysis of proteins. Nat Methods 2006, 3:429-438.
    • (2006) Nat Methods , vol.3 , pp. 429-438
    • Muralidharan, V.1    Muir, T.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.