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Volumn 73, Issue , 2013, Pages 1-16

Using chemical shift perturbation to characterise ligand binding

Author keywords

Chemical shift; Dissociation constant; Docking; Exchange rate; Protein

Indexed keywords

BINDING SITES; DISSOCIATION; DOCKING; FINANCE; HYDROGEN BONDS; LIGANDS; PROTEINS;

EID: 84880167453     PISSN: 00796565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pnmrs.2013.02.001     Document Type: Review
Times cited : (1038)

References (107)
  • 1
    • 0037039335 scopus 로고    scopus 로고
    • Mapping protein-protein interactions in solution by NMR spectroscopy
    • DOI 10.1021/bi011870b
    • E.R.P. Zuiderweg, Mapping protein-protein interactions in solution by NMR spectroscopy, Biochemistry 41 (2002) 1-7. (Pubitemid 34049375)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 1-7
    • Zuiderweg, E.R.P.1
  • 2
    • 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
    • K. Pervushin, R. Riek, G. Wider, K. Wiithrich, 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. USA 94 (1997) 1236612371.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1236612371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wiithrich, K.4
  • 3
    • 34249024639 scopus 로고    scopus 로고
    • Isotopically discriminated NMR spectroscopy: A tool for investigating complex protein interactions in vitro
    • DOI 10.1021/ja070505q
    • A.P. Golovanov, R.T. Blankley, J.M. Avis, W. Bermel, Isotopically discriminated NMR spectroscopy: a tool for investigating complex protein interactions in vitro, J. Am. Chem. Soc. 129 (2007) 6528-6535. (Pubitemid 46799351)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.20 , pp. 6528-6535
    • Golovanov, A.P.1    Blankley, R.T.2    Avis, J.M.3    Bermel, W.4
  • 4
    • 0037009985 scopus 로고    scopus 로고
    • Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations
    • M.A. McCoy, D.F. Wyss, Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations, J. Am. Chem. Soc. 124 (2002) 11758-11763.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11758-11763
    • McCoy, M.A.1    Wyss, D.F.2
  • 5
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • DOI 10.1126/science.274.5292.1531
    • S.B. Shuker, P.J. Hajduk, R.P. Meadows, S.W. Fesik, Discovering high-affinity ligands for proteins: SAR by NMR, Science 274 (1996) 1531-1534. (Pubitemid 26403929)
    • (1996) Science , vol.274 , Issue.5292 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 6
    • 61549100580 scopus 로고    scopus 로고
    • Automated protein structure calculation from NMR data
    • M.P. Williamson, C.J. Craven, Automated protein structure calculation from NMR data, J. Biomol. NMR 43 (2009) 131-143.
    • (2009) J. Biomol. NMR , vol.43 , pp. 131-143
    • Williamson, M.P.1    Craven, C.J.2
  • 7
    • 4744372317 scopus 로고    scopus 로고
    • Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy
    • DOI 10.1021/ja040086m
    • S.G. Zech, E. Olejniczak, P. Hajduk, J. Mack, A.E. McDermot, Characterization of protein-ligand interactions by high-resolution solid-state NMR spectroscopy, J. Am. Chem. Soc. 126 (2004) 13948-13953. (Pubitemid 39447069)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.43 , pp. 13948-13953
    • Zech, S.G.1    Olejniczak, E.2    Hajduk, P.3    Mack, J.4    McDermott, A.E.5
  • 9
    • 70349627256 scopus 로고    scopus 로고
    • Fast and accurate predictions of protein NMR chemical shifts from interatomic distances
    • K.J. Kohlhoff, P. Robustelli, A. Cavalli, X. Salvatella, M. Vendruscolo, Fast and accurate predictions of protein NMR chemical shifts from interatomic distances, J. Am. Chem. Soc. 131 (2009) 13894-13895.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13894-13895
    • Kohlhoff, K.J.1    Robustelli, P.2    Cavalli, A.3    Salvatella, X.4    Vendruscolo, M.5
  • 10
    • 84859575300 scopus 로고    scopus 로고
    • Interpreting protein structural dynamics from NMR chemical shifts
    • P. Robustelli, K.A. Stafford, A.G. Palmer, Interpreting protein structural dynamics from NMR chemical shifts, J. Am. Chem. Soc. 134 (2012) 63656374.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 63656374
    • Robustelli, P.1    Stafford, K.A.2    Palmer, A.G.3
  • 11
    • 0037114648 scopus 로고    scopus 로고
    • Probing multiple effects on 15N, 13Ca, 13Cβ, and 13C' chemical shifts in peptides using density functional theory
    • X.P. Xu, D.A. Case, Probing multiple effects on 15N, 13Ca, 13Cβ, and 13C' chemical shifts in peptides using density functional theory, Biopolymers 65 (2002) 408-423.
    • (2002) Biopolymers , vol.65 , pp. 408-423
    • Xu, X.P.1    Case, D.A.2
  • 12
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach
    • A.C. de Dios, J.G. Pearson, E. Oldfield, Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach, Science 260 (1993) 1491-1496. (Pubitemid 23273262)
    • (1993) Science , vol.260 , Issue.5113 , pp. 1491-1496
    • De Dios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 13
    • 0031576676 scopus 로고    scopus 로고
    • Density functional calculations of proton chemical shifts in model peptides
    • DOI 10.1021/ja9721430
    • D. Sitkoff, D.A. Case, Density functional calculations of proton chemical shifts in model peptides, J. Am. Chem. Soc. 119 (1997) 12262-12273. (Pubitemid 28078714)
    • (1997) Journal of the American Chemical Society , vol.119 , Issue.50 , pp. 12262-12273
    • Sitkoff, D.1    Case, D.A.2
  • 14
    • 44949269218 scopus 로고
    • Empirical comparisons of models for chemical shift calculation in proteins
    • M.P. Williamson, T. Asakura, Empirical comparisons of models for chemical shift calculation in proteins, J. Magn. Reson. Ser. B 101 (1993) 63-71.
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 63-71
    • Williamson, M.P.1    Asakura, T.2
  • 16
    • 0033064395 scopus 로고    scopus 로고
    • C(α) and C(β) carbon-13 chemical shifts in proteins from an empirical database
    • DOI 10.1023/A:1008376710086
    • M. Iwadate, T. Asakura, M.P. Williamson, Ca and Cβ carbon-13 chemical shifts in proteins from an empirical database, J. Biomol. NMR 13 (1999) 199-211. (Pubitemid 29143528)
    • (1999) Journal of Biomolecular NMR , vol.13 , Issue.3 , pp. 199-211
    • Iwadate, M.1    Asakura, T.2    Williamson, M.P.3
  • 17
    • 84985733652 scopus 로고
    • 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly- Gly-X-L-Ala-OH
    • A. Bundi, K. Wüthrich, 1H NMR parameters of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly- Gly-X-L-Ala-OH, Biopolymers 18 (1979) 285-297.
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 18
    • 0029207339 scopus 로고
    • Random coil 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • G. Merutka, H.J. Dyson, P.E. Wright, Random coil 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG, J. Biomol. NMR 5 (1995) 14-24.
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 19
    • 0029181728 scopus 로고
    • 1H 13C and 15N random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects
    • D.S. Wishart, C.G. Bigam, A. Holm, R.S. Hodges, B.D. Sykes, 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. 1. Investigations of nearest-neighbor effects, J. Biomol. NMR 5 (1995) 67-81.
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 21
    • 70450194574 scopus 로고    scopus 로고
    • Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins
    • A. De Simone, A. Cavalli, S.-T.D. Hsu, W. Vranken, M. Vendruscolo, Accurate random coil chemical shifts from an analysis of loop regions in native states of proteins, J. Am. Chem. Soc. 131 (2009) 16332-16333.
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16332-16333
    • De Simone, A.1    Cavalli, A.2    Hsu, S.-T.D.3    Vranken, W.4    Vendruscolo, M.5
  • 22
    • 78650615363 scopus 로고    scopus 로고
    • Sequence-specific random coil chemical shifts of intrinsically disordered proteins
    • K. Tamiola, B. Acar, F.A.A. Mulder, Sequence-specific random coil chemical shifts of intrinsically disordered proteins, J. Am. Chem. Soc. 132 (2010) 18000-18003.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 18000-18003
    • Tamiola, K.1    Acar, B.2    Mulder, F.A.A.3
  • 23
    • 80051704532 scopus 로고    scopus 로고
    • Sequence correction of random coil chemical shifts: Correlation between neighbor correction factors and changes in the Ramachandran distribution
    • M. Kjaergaard, F.M. Poulsen, Sequence correction of random coil chemical shifts: correlation between neighbor correction factors and changes in the Ramachandran distribution, J. Biomol. NMR 50 (2011) 157-165.
    • (2011) J. Biomol. NMR , vol.50 , pp. 157-165
    • Kjaergaard, M.1    Poulsen, F.M.2
  • 24
    • 80051673221 scopus 로고    scopus 로고
    • SHIFTX2: Significantly improved protein chemical shift prediction
    • B. Han, Y. Liu, S.W. Ginzinger, D.S. Wishart, SHIFTX2: significantly improved protein chemical shift prediction, J. Biomol. NMR 50 (2011) 43-57.
    • (2011) J. Biomol. NMR , vol.50 , pp. 43-57
    • Han, B.1    Liu, Y.2    Ginzinger, S.W.3    Wishart, D.S.4
  • 26
    • 84857703407 scopus 로고    scopus 로고
    • Quantitative analysis of multisite protein- ligand interactions by NMR: Binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP
    • M. Arai, J.C. Ferreon, P.E. Wright, Quantitative analysis of multisite protein- ligand interactions by NMR: binding of intrinsically disordered p53 transactivation subdomains with the TAZ2 domain of CBP, J. Am. Chem. Soc. 134 (2012) 3792-3803.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 3792-3803
    • Arai, M.1    Ferreon, J.C.2    Wright, P.E.3
  • 28
    • 0000745765 scopus 로고
    • Determination of dissociation constants of 1:1 complexes from NMR data: Optimization of the experimental setup by statistical analysis of simulated experiments
    • J. Granot, Determination of dissociation constants of 1:1 complexes from NMR data: optimization of the experimental setup by statistical analysis of simulated experiments, J. Magn. Reson. 55 (1983) 216-224.
    • (1983) J. Magn. Reson. , vol.55 , pp. 216-224
    • Granot, J.1
  • 29
    • 35948942349 scopus 로고    scopus 로고
    • NMR methods for the determination of protein-ligand dissociation constants
    • DOI 10.1016/j.pnmrs.2007.04.001, PII S0079656507000258
    • L. Fielding, NMR methods for the determination ofprotein-ligand dissociation constants, Prog. Nucl. Magn. Reson. Spectrosc. 51 (2007) 219-242. (Pubitemid 350064300)
    • (2007) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.51 , Issue.4 , pp. 219-242
    • Fielding, L.1
  • 30
    • 84865185420 scopus 로고    scopus 로고
    • Increased precision for analysis of protein- ligand dissociation constants determined from chemical shift titrations
    • C.J. Markin, L. Spyracopoulos, Increased precision for analysis of protein- ligand dissociation constants determined from chemical shift titrations, J. Biomol. NMR 53 (2012) 125-138.
    • (2012) J. Biomol. NMR , vol.53 , pp. 125-138
    • Markin, C.J.1    Spyracopoulos, L.2
  • 31
    • 29544446689 scopus 로고    scopus 로고
    • Weak protein-protein interactions as probed by NMR spectroscopy
    • DOI 10.1016/j.tibtech.2005.09.006, PII S0167779905002532
    • J. Vaynberg, J. Qin, Weak protein-protein interactions as probed by NMR spectroscopy, Trends Biotechnol. 24 (2006) 22-27. (Pubitemid 43017747)
    • (2006) Trends in Biotechnology , vol.24 , Issue.1 , pp. 22-27
    • Vaynberg, J.1    Qin, J.2
  • 32
    • 0030968136 scopus 로고    scopus 로고
    • Multiple interactions between polyphenols and a salivary proline-rich protein repeat result in complexation and precipitation
    • DOI 10.1021/bi9700328
    • N.J. Baxter, T.H. Lilley, E. Haslam, M.P. Williamson, Multiple interactions between polyphenols and a salivary proline-rich protein repeat result in complexation and precipitation, Biochemistry 36 (1997) 5566-5577. (Pubitemid 27200055)
    • (1997) Biochemistry , vol.36 , Issue.18 , pp. 5566-5577
    • Baxter, N.J.1    Lilley, T.H.2    Haslam, E.3    Williamson, M.P.4
  • 33
    • 77957938043 scopus 로고    scopus 로고
    • Structural origins of pH-dependent chemical shifts in the B1 domain of protein G, Proteins, Proteins: Struct
    • J.H. Tomlinson, V.L. Green, P.J. Baker, M.P. Williamson, Structural origins of pH-dependent chemical shifts in the B1 domain of protein G, Proteins, Proteins: Struct. Funct. Bioinf. 78 (2010) 3000-3016.
    • (2010) Funct. Bioinf. , vol.78 , pp. 3000-3016
    • Tomlinson, J.H.1    Green, V.L.2    Baker, P.J.3    Williamson, M.P.4
  • 34
    • 0033636878 scopus 로고    scopus 로고
    • Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations
    • M.A. McCoy, D.F. Wyss, Alignment of weakly interacting molecules to protein surfaces using simulations of chemical shift perturbations, J. Biomol. NMR 18 (2000) 189-198.
    • (2000) J. Biomol. NMR , vol.18 , pp. 189-198
    • McCoy, M.A.1    Wyss, D.F.2
  • 36
    • 35848958773 scopus 로고    scopus 로고
    • Combined chemical shift changes and amino acid specific chemical shift mapping of protein-protein interactions
    • DOI 10.1007/s10858-007-9197-z
    • F.H. Schumann, H. Riepl, T. Maurer, W. Gronwald, K.-P. Neidig, H.R. Kalbitzer, Combined chemical shift changes and amino acid specific chemical shift mapping of protein-protein interactions, J. Biomol. NMR 39 (2007) 275-289. (Pubitemid 350055750)
    • (2007) Journal of Biomolecular NMR , vol.39 , Issue.4 , pp. 275-289
    • Schumann, F.H.1    Riepl, H.2    Maurer, T.3    Gronwald, W.4    Neidig, K.-P.5    Kalbitzer, H.R.6
  • 37
    • 80051570068 scopus 로고    scopus 로고
    • Quantitative use of chemical shifts for the modeling of protein complexes
    • D. Stratmann, R. Boelens, A.M.J.J. Bonvin, Quantitative use of chemical shifts for the modeling of protein complexes, Proteins: Struct. Funct. Bioinf. 79 (2011) 2662-2670.
    • (2011) Proteins: Struct. Funct. Bioinf. , vol.79 , pp. 2662-2670
    • Stratmann, D.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 39
    • 0032898682 scopus 로고    scopus 로고
    • A robust and cost- effective method for the production of Val, Leu, He81 methyl-protonated 15N-, 13C-, 2H-labeled proteins
    • N.K. Goto, K.H. Gardner, G.A. Mueller, R.C. Willis, L.E. Kay, A robust and cost- effective method for the production of Val, Leu, He81 methyl-protonated 15N-, 13C-, 2H-labeled proteins, J. Biomol. NMR 13 (1999) 369-374.
    • (1999) J. Biomol. NMR , vol.13 , pp. 369-374
    • Goto, N.K.1    Gardner, K.H.2    Mueller, G.A.3    Willis, R.C.4    Kay, L.E.5
  • 40
    • 36049046667 scopus 로고    scopus 로고
    • Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR
    • DOI 10.1016/j.cell.2007.09.039, PII S009286740701269X
    • I. Gelis, A.M.J.J. Bonvin, D. Keramisanou, M. Koukaki, G. Gouridis, S. Karamanou, A. Economou, C.G. Kalodimos, Structural basis for signal- sequence recognition by the translocase motor SecA as determined by NMR, Cell 131 (2007) 756-769. (Pubitemid 350087200)
    • (2007) Cell , vol.131 , Issue.4 , pp. 756-769
    • Gelis, I.1    Bonvin, A.M.J.J.2    Keramisanou, D.3    Koukaki, M.4    Gouridis, G.5    Karamanou, S.6    Economou, A.7    Kalodimos, C.G.8
  • 41
    • 22144435546 scopus 로고    scopus 로고
    • The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy
    • DOI 10.1021/ja052517m
    • D.J. Hamel, F.W. Dahlquist, The contact interface of a 120 kD CheA-CheW complex by methyl TROSY interaction spectroscopy, J. Am. Chem. Soc. 127 (2005) 9676-9677. (Pubitemid 40981519)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.27 , pp. 9676-9677
    • Hamel, D.J.1    Dahlquist, F.W.2
  • 42
    • 34547958577 scopus 로고    scopus 로고
    • Autoinhibition of the HECT-Type Ubiquitin Ligase Smurf2 through Its C2 Domain
    • DOI 10.1016/j.cell.2007.06.050, PII S0092867407009002
    • S. Wiesner, A.A. Ogunjimi, H.-R. Wang, D. Rotin, F. Sicheri, J.L. Wrana, J.D. Forman-Kay, Autoinhibition of the HECT-Type ubiquitin ligase smurf2 through its C2 domain, Cell 130 (2007) 651-662. (Pubitemid 47268058)
    • (2007) Cell , vol.130 , Issue.4 , pp. 651-662
    • Wiesner, S.1    Ogunjimi, A.A.2    Wang, H.-R.3    Rotin, D.4    Sicheri, F.5    Wrana, J.L.6    Forman-Kay, J.D.7
  • 44
    • 0035154869 scopus 로고    scopus 로고
    • Calmodulin binding properties of peptide analogues and fragments of the calmodulin-binding domain of simian immunodeficiency virus transmembrane glycoprotein 41
    • DOI 10.1002/1097-0282(200101)58:1<50::AID-BIP60>3.0.CO;2-S
    • T. Yuan, S. Tencza, T.A. Meitzner, R.C. Montelaro, H.J. Vogel, Calmodulin binding properties of peptide analogues and fragments of the calmodulin- binding domain of simian immunodeficiency virus transmembrane glycoprotein 41, Biopolymers 58 (2001) 50-62. (Pubitemid 32064067)
    • (2001) Biopolymers , vol.58 , Issue.1 , pp. 50-62
    • Yuan, T.1    Tencza, S.2    Mietzner, T.A.3    Montelaro, R.C.4    Vogel, H.J.5
  • 46
    • 84859406875 scopus 로고    scopus 로고
    • Methionine scanning as an NMR tool for detecting and analyzing biomolecular interaction surfaces
    • M.C. Stoffregen, M.M. Schwer, F.A. Renschler, S. Wiesner, Methionine scanning as an NMR tool for detecting and analyzing biomolecular interaction surfaces, Structure 20 (2012) 573-581.
    • (2012) Structure , vol.20 , pp. 573-581
    • Stoffregen, M.C.1    Schwer, M.M.2    Renschler, F.A.3    Wiesner, S.4
  • 47
    • 84858981531 scopus 로고    scopus 로고
    • Unraveling complex small- molecule binding mechanisms by using simple NMR spectroscopy
    • M. Quinternet, J.-P. Starck, M.-A. Delsuc, B. Kieffer, Unraveling complex small- molecule binding mechanisms by using simple NMR spectroscopy, Chem. Eur. J. 18 (2012) 3969-3974.
    • (2012) Chem. Eur. J. , vol.18 , pp. 3969-3974
    • Quinternet, M.1    Starck, J.-P.2    Delsuc, M.-A.3    Kieffer, B.4
  • 48
    • 0034765285 scopus 로고    scopus 로고
    • Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity
    • DOI 10.1038/nsb1101-947
    • S.Y. Stevens, S. Sanker, C. Kent, E.R.P. Zuiderweg, Delineation of the allosteric mechanism of a cytidylyltransferase exhibiting negative cooperativity, Nature Struct. Biol. 8 (2001) 947-952. (Pubitemid 33034601)
    • (2001) Nature Structural Biology , vol.8 , Issue.11 , pp. 947-952
    • Stevens, S.Y.1    Sanker, S.2    Kent, C.3    Zuiderweg, E.R.P.4
  • 49
    • 0029563931 scopus 로고
    • Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy
    • DOI 10.1021/bi00051a007
    • C.H. Hardman, R.W. Broadhurst, A.R.C. Raine, K.D. Grasser, J.O. Thomas, E.D. Laue, Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy, Biochemistry 34 (1995) 16596-16607. (Pubitemid 26011782)
    • (1995) Biochemistry , vol.34 , Issue.51 , pp. 16596-16607
    • Hardman, C.H.1    Broadhurst, R.W.2    Raine, A.R.C.3    Grasser, K.D.4    Thomas, J.O.5    Laue, E.D.6
  • 50
    • 0033522480 scopus 로고    scopus 로고
    • Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding
    • DOI 10.1093/emboj/18.9.2563
    • F.H.T. Allain, Y.M. Yen, J.E. Masse, P. Schultze, T. Dieckmann, R.C. Johnson, J. Feigon, Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding, EMBO J. 18 (1999) 2563-2579. (Pubitemid 29213287)
    • (1999) EMBO Journal , vol.18 , Issue.9 , pp. 2563-2579
    • Allain, F.H.-T.1    Yen, Y.-M.2    Masse, J.E.3    Schultze, P.4    Dieckmann, T.5    Johnson, R.C.6    Feigon, J.7
  • 52
    • 0030666085 scopus 로고    scopus 로고
    • Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation
    • DOI 10.1021/bi9712091
    • R.A. Williamson, M.D. Carr, T.A. Frenkiel, J. Feeney, R.B. Freedman, Mapping the binding site for matrix metalloproteinase on the N-terminal domain of the tissue inhibitor of metalloproteinases-2 by NMR chemical shift perturbation, Biochemistry 36 (1997) 13882-13889. (Pubitemid 27494895)
    • (1997) Biochemistry , vol.36 , Issue.45 , pp. 13882-13889
    • Williamson, R.A.1    Carr, M.D.2    Frenkiel, T.A.3    Feeney, J.4    Freedman, R.B.5
  • 54
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • D.S. Wishart, B.D. Sykes, F.M. Richards, Relationship between nuclear magnetic resonance chemical shift and protein secondary structure, J. Mol. Biol. 222 (1991) 311-333. (Pubitemid 121004009)
    • (1991) Journal of Molecular Biology , vol.222 , Issue.2 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 55
    • 0036786190 scopus 로고    scopus 로고
    • Solution structure of a novel chromoprotein derived from apo- Neocarzinostatin and a synthetic chromophore
    • M.D. Urbaniak, F.W. Muskett, M.D. Finucane, S. Caddick, D.N. Woolfson, Solution structure of a novel chromoprotein derived from apo- Neocarzinostatin and a synthetic chromophore, Biochemistry 41 (2002) 11731-11739.
    • (2002) Biochemistry , vol.41 , pp. 11731-11739
    • Urbaniak, M.D.1    Muskett, F.W.2    Finucane, M.D.3    Caddick, S.4    Woolfson, D.N.5
  • 56
    • 0000178351 scopus 로고    scopus 로고
    • A family IIb xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity
    • DOI 10.1016/S0969-2126(99)80108-7
    • P.J. Simpson, D.N. Bolam, A. Cooper, A. Ciruela, G.P. Hazlewood, H.J. Gilbert, M.P. Williamson, A family lib xylan-binding domain has a similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity, Struct. Fold. Des. 7 (1999) 853-864. (Pubitemid 29329855)
    • (1999) Structure , vol.7 , Issue.7 , pp. 853-864
    • Simpson, P.J.1    Bolam, D.N.2    Cooper, A.3    Ciruela, A.4    Hazlewood, G.P.5    Gilbert, H.J.6    Williamson, M.P.7
  • 59
    • 0037426325 scopus 로고    scopus 로고
    • Elucidation of the e-6 subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy
    • DOI 10.1021/bi0205451
    • E.F. DeRose, T. Darden, S. Harvey, S. Gabel, F.W. Perrino, R.M. Schaaper, R.E. London, Elucidation of the e-6 subunit interface of Escherichia coli DNA polymerase III by NMR spectroscopy, Biochemistry 42 (2003) 3635-3644. (Pubitemid 36402656)
    • (2003) Biochemistry , vol.42 , Issue.13 , pp. 3635-3644
    • DeRose, E.F.1    Darden, T.2    Harvey, S.3    Gabel, S.4    Perrino, F.W.5    Schaaper, R.M.6    London, R.E.7
  • 60
    • 0141750584 scopus 로고    scopus 로고
    • Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats
    • DOI 10.1016/j.jmb.2003.08.050
    • J. Morrison, J.C. Yang, M. Stewart, D. Neuhaus, Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats, J. Mol. Biol. 333 (2003) 587-603. (Pubitemid 37222408)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.3 , pp. 587-603
    • Morrison, J.1    Yang, J.-C.2    Stewart, M.3    Neuhaus, D.4
  • 61
    • 0036290278 scopus 로고    scopus 로고
    • Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli
    • DOI 10.1006/jmbi.2001.5388
    • H. Lüttgen, R. Robelek, R. Mühlberger, T. Diercks, S.C. Schuster, P. Köhler, H. Kessler, A. Bacher, G. Richter, Transcriptional regulation by antitermination. Interaction of RNA with NusB protein and NusB/NusE protein complex of Escherichia coli, J. Mol. Biol. 316 (2002) 875-885. (Pubitemid 34722127)
    • (2002) Journal of Molecular Biology , vol.316 , Issue.4 , pp. 875-885
    • Luttgen, H.1    Robelek, R.2    Muhlberger, R.3    Diercks, T.4    Schuster, S.C.5    Kohler, P.6    Kessler, H.7    Bacher, A.8    Richter, G.9
  • 62
    • 0000840313 scopus 로고
    • Chemical shift and linewidth characteristics of reversibly bound ligands
    • R.E. London, Chemical shift and linewidth characteristics of reversibly bound ligands, J. Magn. Reson. Ser. A 104 (1993) 190-196.
    • (1993) J. Magn. Reson. Ser. A , vol.104 , pp. 190-196
    • London, R.E.1
  • 63
    • 0000337195 scopus 로고
    • Dependence of NMR lineshape analysis upon chemical rates and mechanisms: Implications for enzyme histidine titrations
    • J.L. Sudmeier, J.L. Evelhoch, N.B.H. Jonsson, Dependence of NMR lineshape analysis upon chemical rates and mechanisms: implications for enzyme histidine titrations, J. Magn. Reson. 40 (1980) 377-390.
    • (1980) J. Magn. Reson. , vol.40 , pp. 377-390
    • Sudmeier, J.L.1    Evelhoch, J.L.2    Jonsson, N.B.H.3
  • 64
    • 84865166917 scopus 로고    scopus 로고
    • NMR line shapes and multi-state binding equilibria
    • E.L. Kovrigin, NMR line shapes and multi-state binding equilibria, J. Biomol. MR 53 (2012) 257-270.
    • (2012) J. Biomol. MR , vol.53 , pp. 257-270
    • Kovrigin, E.L.1
  • 65
    • 0001559701 scopus 로고
    • Effects of intermediate exchange processes on the estimation of equilibrium constants by NMR
    • J. Feeney, J.G. Batchelor, J.P. Albrand, G.C.K. Roberts, Effects of intermediate exchange processes on the estimation of equilibrium constants by NMR, J. Magn. Reson. 33 (1979) 519-529.
    • (1979) J. Magn. Reson. , vol.33 , pp. 519-529
    • Feeney, J.1    Batchelor, J.G.2    Albrand, J.P.3    Roberts, G.C.K.4
  • 66
    • 79955874670 scopus 로고    scopus 로고
    • Structure-function analysis of a CvNH-LysM lectin expressed during plant infection by the rice blast fungus Magnaporthe oryzae
    • L.M.I. Koharudin, A.R. Viscomi, B. Montanini, M.J. Kershaw, N.J. Talbot, S. Ottonello, A.M. Gronenborn, Structure-function analysis of a CvNH-LysM lectin expressed during plant infection by the rice blast fungus Magnaporthe oryzae, Structure 19 (2011) 662-674.
    • (2011) Structure , vol.19 , pp. 662-674
    • Koharudin, L.M.I.1    Viscomi, A.R.2    Montanini, B.3    Kershaw, M.J.4    Talbot, N.J.5    Ottonello, S.6    Gronenborn, A.M.7
  • 67
    • 0034016522 scopus 로고    scopus 로고
    • NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor
    • C. McInnes, S. Grothe, M. O'Connor-McCourt, B.D. Sykes, NMR study of the differential contributions of residues of transforming growth factor alpha to association with its receptor, Prot. Eng. 13 (2000) 143-147. (Pubitemid 30237588)
    • (2000) Protein Engineering , vol.13 , Issue.3 , pp. 143-147
    • McInnes, C.1    Grothe, S.2    O'Connor-McCourt, M.3    Sykes, B.D.4
  • 68
    • 0024404656 scopus 로고
    • Nuclear magnetic resonance line-shape analysis and determination of exchange rates
    • DOI 10.1016/0076-6879(89)76016-X
    • B.D.N. Rao, Nuclear magnetic resonance line-shape analysis and determination of exchange rates, Meth. Enzymol. 176 (1989) 279-311. (Pubitemid 20003086)
    • (1989) Methods in Enzymology , vol.176 , pp. 279-311
    • Rao, B.D.N.1
  • 71
    • 30744449974 scopus 로고    scopus 로고
    • NMR indicates that the small molecule RITA does not block p53-MDM2 binding in vitro [1]
    • DOI 10.1038/nm1105-1135, PII NM11051135
    • M. Krajewski, P. Ozdowy, L. D'Silva, U. Rothweiler, T.A. Holak, NMR indicates that the small molecule RITA does not block p53-MDM2 binding in vitro, Nature Med. 11 (2005) 1135-1136. (Pubitemid 43093648)
    • (2005) Nature Medicine , vol.11 , Issue.11 , pp. 1135-1136
    • Krajewski, M.1    Ozdowy, P.2    D'Silva, L.3    Rothweiler, U.4    Holak, T.A.5
  • 73
    • 0022558846 scopus 로고
    • 1H Resonance assignments and coenzyme-induced conformational changes
    • S.J. Hammond, B. Birdsall, M.S. Searle, G.C.K. Roberts, J. Feeney, Dihydrofolate reductase 1H resonance assignments and coenzyme-induced conformational changes, J. Mol. Biol. 188 (1986) 81-97. (Pubitemid 16083704)
    • (1986) Journal of Molecular Biology , vol.188 , Issue.1 , pp. 81-97
    • Hammond, S.J.1    Birdsall, B.2    Searler, M.S.3
  • 74
    • 0032113850 scopus 로고    scopus 로고
    • Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino-terminal zinc finger domains from transcription factor IIIA
    • M.P. Foster, D.S. Wuttke, K.R. Clemens, W. Jahnke, I. Radhakrishnan, L. Tennant, M. Reymond, J. Chung, P.E. Wright, Chemical shift as a probe of molecular interfaces: NMR studies of DNA binding by the three amino- terminal zinc finger domains from transcription factor IIIA, J. Biomol. NMR 12 (1998) 51-71. (Pubitemid 128512834)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.1 , pp. 51-71
    • Foster, M.P.1    Wuttke, D.S.2    Clemens, K.R.3    Jahnke, W.4    Radhakrishnan, I.5    Tennant, L.6    Reymond, M.7    Chung, J.8    Wright, P.E.9
  • 75
    • 0029840073 scopus 로고    scopus 로고
    • Complexes formed between calmodulin and the antagonists J-8 and TFP in solution
    • DOI 10.1021/bi9605043
    • C.J. Craven, B. Whitehead, S.K.A. Jones, E. Thulin, G.M. Blackburn, J.P. Waltho, Complexes formed between calmodulin and the antagonists J-8 and TFP in solution, Biochemistry 35 (1996) 10287-10299. (Pubitemid 26277287)
    • (1996) Biochemistry , vol.35 , Issue.32 , pp. 10287-10299
    • Craven, C.J.1    Whitehead, B.2    Jones, S.K.A.3    Thulin, E.4    Blackburn, G.M.5    Waltho, J.P.6
  • 76
    • 2642605367 scopus 로고    scopus 로고
    • Demonstration of protein-protein interaction specificity by NMR chemical shift mapping
    • P. Rajagopal, E.B. Waygood, J. Reizer, M.H. Saier, R.E. Klevit, Demonstration of protein-protein interaction specificity by NMR chemical shift mapping, Protein Sci. 6 (1997) 2624-2627. (Pubitemid 28006699)
    • (1997) Protein Science , vol.6 , Issue.12 , pp. 2624-2627
    • Rajagopal, P.1    Bruce Waygood, E.2    Reizer, J.3    Saier Jr., M.H.4    Klevit, R.E.5
  • 77
    • 0038470801 scopus 로고    scopus 로고
    • Transient protein interactions studied by NMR spectroscopy: The case of cytochrome c and adrenodoxin
    • DOI 10.1021/bi0342968
    • J.A.R. Worrall, W. Reinle, R. Bernhardt, M. Ubbink, Transient protein interactions studied by NMR spectroscopy: the case of cytochrome c and adrenodoxin, Biochemistry 42 (2003) 7068-7076. (Pubitemid 36706490)
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7068-7076
    • Worrall, J.A.R.1    Reinle, W.2    Bernhardt, R.3    Ubbink, M.4
  • 78
    • 77949523858 scopus 로고    scopus 로고
    • Auto-FACE: An NMR based binding site mapping program for fast chemical exchange protein-ligand systems
    • J. Krishnamoorthy, V.C.K. Yu, Y.-K. Mok, Auto-FACE: an NMR based binding site mapping program for fast chemical exchange protein-ligand systems, PLoS ONE 5 (2010) e8943.
    • (2010) PLoS ONE , vol.5
    • Krishnamoorthy, J.1    Yu, V.C.K.2    Mok, Y.-K.3
  • 79
    • 84866064390 scopus 로고    scopus 로고
    • Determining binding constants from 1H NMR titration data using global and local methods: A case study using [n]polynorbornane-based anion hosts
    • A.J. Lowe, F.M. Pfeffer, P. Thordarson, Determining binding constants from 1H NMR titration data using global and local methods: a case study using [n]polynorbornane-based anion hosts, Supramol. Chem. 24 2012: 585-594.
    • (2012) Supramol. Chem. , vol.24 , pp. 585-594
    • Lowe, A.J.1    Pfeffer, F.M.2    Thordarson, P.3
  • 80
    • 84871078073 scopus 로고    scopus 로고
    • Principal component analysis of chemical shift perturbation data of a multiple-ligand-binding system for elucidation of respective binding mechanism
    • T. Konuma, Y.-H. Lee, Y. Goto, K. Sakurai, Principal component analysis of chemical shift perturbation data of a multiple-ligand-binding system for elucidation of respective binding mechanism, Proteins: Struct. Funct. Bioinf. 81 (2013) 107-118.
    • (2013) Proteins: Struct. Funct. Bioinf. , vol.81 , pp. 107-118
    • Konuma, T.1    Lee, Y.-H.2    Goto, Y.3    Sakurai, K.4
  • 83
    • 83555179143 scopus 로고    scopus 로고
    • On the use of distance constraints in protein-protein docking computations
    • E.S.C. Shih, M.-J. Hwang, On the use of distance constraints in protein-protein docking computations, Proteins: Struct. Funct. Bioinf. 80 (2012) 194-205.
    • (2012) Proteins: Struct. Funct. Bioinf. , vol.80 , pp. 194-205
    • Shih, E.S.C.1    Hwang, M.-J.2
  • 85
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • DOI 10.1021/ja026939x
    • C. Domínguez, R. Boelens, A.M.J.J. Bonvin, HADDOCK: A protein-protein docking approach based on biochemical or biophysical information, J. Am. Chem. Soc. 125 (2003) 1731-1737. (Pubitemid 36232568)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.7 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.J.J.3
  • 88
    • 0034808070 scopus 로고    scopus 로고
    • A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data
    • DOI 10.1110/ps.07501
    • X.J. Morelli, P.N. Palma, F. Guerlesquin, A.C. Rigby, A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data, Protein Sci. 10 (2001) 2131-2137. (Pubitemid 32911232)
    • (2001) Protein Science , vol.10 , Issue.10 , pp. 2131-2137
    • Morelli, X.J.1    Palma, P.N.2    Guerlesquin, F.3    Rigby, A.C.4
  • 89
    • 40149093773 scopus 로고    scopus 로고
    • Rapid protein-ligand costructures using chemical shift perturbations
    • DOI 10.1021/ja0737974
    • J. Stark, R. Powers, Rapid protein-ligand costructures using chemical shift perturbations, J. Am. Chem. Soc. 130 (2008) 535-545. (Pubitemid 351455567)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.2 , pp. 535-545
    • Stark, J.1    Powers, R.2
  • 90
    • 0037433504 scopus 로고    scopus 로고
    • 1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
    • DOI 10.1021/ja028893d
    • G.M. Clore, C.D. Schwieters, Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 'HN/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics, J. Am. Chem. Soc. 125 (2003) 2902-2912. (Pubitemid 36512515)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.10 , pp. 2902-2912
    • Clore, G.M.1    Schwieters, C.D.2
  • 91
    • 76949101712 scopus 로고    scopus 로고
    • SAMPLEX: Automatic mapping of perturbed and unperturbed regions of proteins and complexes
    • M. Krzeminski, K. Loth, R. Boelens, A.M.J.J. Bonvin, SAMPLEX: automatic mapping of perturbed and unperturbed regions of proteins and complexes, BMC Bioinf. 11 (2010) 51.
    • (2010) BMC Bioinf. , vol.11 , pp. 51
    • Krzeminski, M.1    Loth, K.2    Boelens, R.3    Bonvin, A.M.J.J.4
  • 92
    • 0034673316 scopus 로고    scopus 로고
    • The use of differential chemical shifts for determining the binding site location and orientation of protein-bound ligands [14]
    • DOI 10.1021/ja993921m
    • A. Medek, P.J. Hajduk, J. Mack, S.W. Fesik, The use of differential chemical shifts for determining the binding site location and orientation of protein- bound ligands, J. Am. Chem. Soc. 122 (2000) 1241-1242. (Pubitemid 30117473)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.6 , pp. 1241-1242
    • Medek, A.1    Hajduk, P.J.2    Mack, J.3    Fesik, S.W.4
  • 93
    • 0037138678 scopus 로고    scopus 로고
    • A novel approach for characterizing protein ligand complexes: Molecular basis for specificity of small-molecule Bcl-2 inhibitors
    • DOI 10.1021/ja011239y
    • A.A. Lugovskoy, A.I. Degterev, A.F. Fahmy, P. Zhou, J.D. Gross, J.Y. Yuan, G. Wagner, A novel approach for characterizing protein ligand complexes: molecular basis for specificity of small-molecule Bcl-2 inhibitors, J. Am. Chem. Soc. 124 (2002) 1234-1240. (Pubitemid 34169130)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.7 , pp. 1234-1240
    • Lugovskoy, A.A.1    Degterev, A.I.2    Fahmy, A.F.3    Zhou, P.4    Gross, J.D.5    Yuan, J.6    Wagner, G.7
  • 97
    • 0037070536 scopus 로고    scopus 로고
    • Structures of protein - Protein complexes are docked using only NMR restraints from residual dipolar coupling and chemical shift perturbations
    • DOI 10.1021/ja017242z
    • M.A. McCoy, D.F. Wyss, Structures of protein-protein complexes are docked using only NMR restraints from residual dipolar coupling and chemical shift perturbations, J. Am. Chem. Soc. 124 (2002) 2104-2105. (Pubitemid 34267084)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.10 , pp. 2104-2105
    • McCoy, M.A.1    Wyss, D.F.2
  • 98
    • 43049083331 scopus 로고    scopus 로고
    • 1H NMR chemical shift
    • DOI 10.1021/jm701194r
    • M. Cioffi, C.A. Hunter, M.J. Packer, A. Spitaleri, Determination of protein- ligand binding modes using complexation-induced changes in 1H NMR chemical shift, J. Med. Chem. 51 (2008) 2512-2517. (Pubitemid 351628512)
    • (2008) Journal of Medicinal Chemistry , vol.51 , Issue.8 , pp. 2512-2517
    • Ciofli, M.1    Hunter, C.A.2    Packer, M.J.3    Spitaleri, A.4
  • 99
    • 49449095976 scopus 로고    scopus 로고
    • Influence of conformational flexibility on complexation-induced changes in chemical shift in a neocarzinostatin protein - Ligand complex
    • M. Cioffi, C.A. Hunter, M.J. Packer, Influence of conformational flexibility on complexation-induced changes in chemical shift in a neocarzinostatin protein - ligand complex, J. Med. Chem. 51 (2008) 4488-4495.
    • (2008) J. Med. Chem. , vol.51 , pp. 4488-4495
    • Cioffi, M.1    Hunter, C.A.2    Packer, M.J.3
  • 100
    • 57549112574 scopus 로고    scopus 로고
    • Use of quantitative 1H NMR chemical shift changes for ligand docking into barnase
    • M. Cioffi, C.A. Hunter, M. Pandya, M.J. Packer, M.P. Williamson, Use of quantitative 1H NMR chemical shift changes for ligand docking into barnase, J. Biomol. NMR 43 (2009) 11-19.
    • (2009) J. Biomol. NMR , vol.43 , pp. 11-19
    • Cioffi, M.1    Hunter, C.A.2    Pandya, M.3    Packer, M.J.4    Williamson, M.P.5
  • 102
    • 17644384789 scopus 로고    scopus 로고
    • Validation of the binding site structure of the cellular retinol-binding protein (CRBP) by ligand NMR chemical shift perturbations
    • DOI 10.1021/ja042616k
    • B. Wang, K.M. Merz, Validation of the binding site structure of the cellular retinol-binding protein (CRBP) by ligand NMR chemical shift perturbations, J. Am. Chem. Soc. 127 (2005) 5310-5311. (Pubitemid 40569829)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.15 , pp. 5310-5311
    • Wang, B.1    Merz Jr., K.M.2
  • 103
    • 70350508200 scopus 로고    scopus 로고
    • Steering protein-ligand docking with quantitative NMR chemical shift perturbations
    • D. González-Ruiz, H. Gohlke, Steering protein-ligand docking with quantitative NMR chemical shift perturbations, J. Chem. Inf. Model. 49 (2009) 2260-2271.
    • (2009) J. Chem. Inf. Model. , vol.49 , pp. 2260-2271
    • González-Ruiz, D.1    Gohlke, H.2
  • 104
    • 0038407231 scopus 로고    scopus 로고
    • 15N chemical shifts
    • DOI 10.1023/A:1023812930288
    • S. Neal, A.M. Nip, H. Zhang, D.S. Wishart, Rapid and accurate calculation of protein 1H, 13C and 15N chemical shifts, J. Biomol. NMR 26 (2003) 215-240. (Pubitemid 36758442)
    • (2003) Journal of Biomolecular NMR , vol.26 , Issue.3 , pp. 215-240
    • Neal, S.1    Nip, A.M.2    Zhang, H.3    Wishart, D.S.4
  • 105
    • 56749151048 scopus 로고    scopus 로고
    • Structure determination of protein-protein complexes using NMR chemical shifts: Case of an endonuclease colicin-immunity protein complex
    • R.W. Montalvao, A. Cavalli, X. Salvatella, T.L. Blundell, M. Vendruscolo, Structure determination of protein-protein complexes using NMR chemical shifts: case of an endonuclease colicin-immunity protein complex, J. Am. Chem. Soc. 130 (2008) 15990-15996.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 15990-15996
    • Montalvao, R.W.1    Cavalli, A.2    Salvatella, X.3    Blundell, T.L.4    Vendruscolo, M.5
  • 106
    • 79960909252 scopus 로고    scopus 로고
    • Using chemical shifts to determine structural changes in proteins upon complex formation
    • A. Cavalli, R.W. Montalvao, M. Vendruscolo, Using chemical shifts to determine structural changes in proteins upon complex formation, J. Phys. Chem. B 115 (2011) 9491-9494.
    • (2011) J. Phys. Chem. B , vol.115 , pp. 9491-9494
    • Cavalli, A.1    Montalvao, R.W.2    Vendruscolo, M.3
  • 107
    • 44949260034 scopus 로고    scopus 로고
    • Probing electric fields in proteins in solution by NMR spectroscopy
    • DOI 10.1002/prot.21929
    • M.A.S. Hass, M.R. Jensen, J.J. Led, Probing electric fields in proteins in solution by NMR spectroscopy, Proteins: Struct. Funct. Bioinf. 72 (2008) 333-343. (Pubitemid 351809171)
    • (2008) Proteins: Structure, Function and Genetics , vol.72 , Issue.1 , pp. 333-343
    • Hass, M.A.S.1    Jensen, M.R.2    Led, J.J.3


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