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Volumn 377, Issue 5, 2008, Pages 1474-1487

Compensatory and Long-Range Changes in Picosecond-Nanosecond Main-Chain Dynamics upon Complex Formation: 15N Relaxation Analysis of the Free and Bound States of the Ubiquitin-like Domain of Human Plexin-B1 and the Small GTPase Rac1

Author keywords

allostery; cell signaling; NMR; protein protein interactions; spin relaxation

Indexed keywords

NITROGEN 15; PLEXIN; PLEXIN B1; RAC1 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 40849102348     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.01.081     Document Type: Article
Times cited : (45)

References (62)
  • 1
    • 0020698476 scopus 로고
    • Dynamics of proteins: elements and function
    • Karplus M., and McCammon J.A. Dynamics of proteins: elements and function. Annu. Rev. Biochem. 53 (1983) 263-300
    • (1983) Annu. Rev. Biochem. , vol.53 , pp. 263-300
    • Karplus, M.1    McCammon, J.A.2
  • 2
    • 32344434479 scopus 로고    scopus 로고
    • The changing landscape of protein allostery
    • Swain J.F., and Gierasch L.M. The changing landscape of protein allostery. Curr. Opin. Struct. Biol. 16 (2006) 102-108
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 102-108
    • Swain, J.F.1    Gierasch, L.M.2
  • 3
    • 14844361989 scopus 로고    scopus 로고
    • NMR studies of protein structure and dynamics
    • Kay L.E. NMR studies of protein structure and dynamics. J. Magn. Reson. 173 (2005) 193-207
    • (2005) J. Magn. Reson. , vol.173 , pp. 193-207
    • Kay, L.E.1
  • 4
    • 0034984208 scopus 로고    scopus 로고
    • NMR probes of molecular dynamics: overview and comparison with other techniques
    • Palmer III A.G. NMR probes of molecular dynamics: overview and comparison with other techniques. Annu. Rev. Biophys. Biomol. Struct. 30 (2001) 129-155
    • (2001) Annu. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 129-155
    • Palmer III, A.G.1
  • 5
    • 0032824805 scopus 로고    scopus 로고
    • Folding funnels and binding mechanisms
    • Ma B., Kumar S., Tsai C.J., and Nussinov R. Folding funnels and binding mechanisms. Protein Eng. 12 (1999) 713-720
    • (1999) Protein Eng. , vol.12 , pp. 713-720
    • Ma, B.1    Kumar, S.2    Tsai, C.J.3    Nussinov, R.4
  • 6
    • 33751086423 scopus 로고    scopus 로고
    • Visualization of transient encounter complexes in protein-protein association
    • Tang C., Iwahara J., and Clore G.M. Visualization of transient encounter complexes in protein-protein association. Nature 444 (2006) 383-386
    • (2006) Nature , vol.444 , pp. 383-386
    • Tang, C.1    Iwahara, J.2    Clore, G.M.3
  • 7
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr D.D., McElheny D., Dyson H.J., and Wright P.E. The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313 (2006) 1638-1642
    • (2006) Science , vol.313 , pp. 1638-1642
    • Boehr, D.D.1    McElheny, D.2    Dyson, H.J.3    Wright, P.E.4
  • 8
    • 12144259853 scopus 로고    scopus 로고
    • NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain
    • Finerty P.J., Mittermaier A.K., Muhandiram R., Kay L.E., and Forman-Kay J.D. NMR dynamics-derived insights into the binding properties of a peptide interacting with an SH2 domain. Biochemistry 44 (2005) 694-703
    • (2005) Biochemistry , vol.44 , pp. 694-703
    • Finerty, P.J.1    Mittermaier, A.K.2    Muhandiram, R.3    Kay, L.E.4    Forman-Kay, J.D.5
  • 9
    • 0038219675 scopus 로고    scopus 로고
    • Temperature dependence of the backbone dynamics of ribonuclease A in the ground state and bound to the inhibitor 5′-phosphothymidine (3′-5′)pyrophosphate adenosine 3′-phosphate
    • Kovrigin E.L., Cole R., and Loria J.P. Temperature dependence of the backbone dynamics of ribonuclease A in the ground state and bound to the inhibitor 5′-phosphothymidine (3′-5′)pyrophosphate adenosine 3′-phosphate. Biochemistry 42 (2003) 5279-5291
    • (2003) Biochemistry , vol.42 , pp. 5279-5291
    • Kovrigin, E.L.1    Cole, R.2    Loria, J.P.3
  • 10
    • 0035798419 scopus 로고    scopus 로고
    • The role of backbone motions in ligand binding to the c-Src SH3 domain
    • Wang C., Pawley N.H., and Nicholson L.K. The role of backbone motions in ligand binding to the c-Src SH3 domain. J. Mol. Biol. 313 (2001) 873-887
    • (2001) J. Mol. Biol. , vol.313 , pp. 873-887
    • Wang, C.1    Pawley, N.H.2    Nicholson, L.K.3
  • 11
    • 0033988897 scopus 로고    scopus 로고
    • Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex
    • Lee A.L., Kinnear S.A., and Wand A.J. Redistribution and loss of side chain entropy upon formation of a calmodulin-peptide complex. Nat. Struct. Biol. 7 (2000) 72-77
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 72-77
    • Lee, A.L.1    Kinnear, S.A.2    Wand, A.J.3
  • 12
    • 33748781457 scopus 로고    scopus 로고
    • The dynamic energy landscape of dihydrofolate reductase catalysis
    • Boehr D.D., McElheny D., Dyson J.H., and Wright P.E. The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313 (2006) 1638-1641
    • (2006) Science , vol.313 , pp. 1638-1641
    • Boehr, D.D.1    McElheny, D.2    Dyson, J.H.3    Wright, P.E.4
  • 13
    • 0037470616 scopus 로고    scopus 로고
    • Increased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3
    • Arumugam S., Gao G., Patton B.L., Semenchenko V., Brew K., and Van Doren S.R. Increased backbone mobility in beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3. J. Mol. Biol. 327 (2003) 719-734
    • (2003) J. Mol. Biol. , vol.327 , pp. 719-734
    • Arumugam, S.1    Gao, G.2    Patton, B.L.3    Semenchenko, V.4    Brew, K.5    Van Doren, S.R.6
  • 14
    • 0036967268 scopus 로고    scopus 로고
    • Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding
    • Akerud T., Thulin E., Van Etten R.L., and Akke M. Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding. J. Mol. Biol. 322 (2002) 137-152
    • (2002) J. Mol. Biol. , vol.322 , pp. 137-152
    • Akerud, T.1    Thulin, E.2    Van Etten, R.L.3    Akke, M.4
  • 15
    • 20544437208 scopus 로고    scopus 로고
    • Main chain and side chain dynamics of the ubiquitin conjugating enzyme variant human Mms2 in the free and ubiquitin-bound states
    • Spyracopoulos L., Lewis M.J., and Saltibus L.F. Main chain and side chain dynamics of the ubiquitin conjugating enzyme variant human Mms2 in the free and ubiquitin-bound states. Biochemistry 44 (2005) 8770-8781
    • (2005) Biochemistry , vol.44 , pp. 8770-8781
    • Spyracopoulos, L.1    Lewis, M.J.2    Saltibus, L.F.3
  • 16
    • 38849144628 scopus 로고    scopus 로고
    • NMR relaxation study of the complex formed between CBP and the activation domain of the nuclear hormone receptor coactivator ACTR
    • Ebert M.O., Bae S.H., Dyson H.J., and Wright P.E. NMR relaxation study of the complex formed between CBP and the activation domain of the nuclear hormone receptor coactivator ACTR. Biochemistry 47 (2008) 1299-1308
    • (2008) Biochemistry , vol.47 , pp. 1299-1308
    • Ebert, M.O.1    Bae, S.H.2    Dyson, H.J.3    Wright, P.E.4
  • 17
    • 0035807930 scopus 로고    scopus 로고
    • 15N-labeled peptide derived from P21-activated kinase bound to Cdc42Hs, GMPPCP
    • 15N-labeled peptide derived from P21-activated kinase bound to Cdc42Hs, GMPPCP. Biochemistry 40 (2001) 14368-14375
    • (2001) Biochemistry , vol.40 , pp. 14368-14375
    • Gizachew, D.1    Oswald, R.E.2
  • 19
    • 1842505060 scopus 로고    scopus 로고
    • A two-state allosteric model for autoinhibition rationalizes WASP signal integration and targeting
    • Buck M., Xu W., and Rosen M.K. A two-state allosteric model for autoinhibition rationalizes WASP signal integration and targeting. J. Mol. Biol. 338 (2004) 271-285
    • (2004) J. Mol. Biol. , vol.338 , pp. 271-285
    • Buck, M.1    Xu, W.2    Rosen, M.K.3
  • 20
    • 3543068747 scopus 로고    scopus 로고
    • Backbone dynamics of an oncogenic mutant of Cdc42Hs shows increased flexibility at the nucleotide-binding site
    • Adams P.D., Loh A.P., and Oswald R.E. Backbone dynamics of an oncogenic mutant of Cdc42Hs shows increased flexibility at the nucleotide-binding site. Biochemistry 43 (2004) 9968-9977
    • (2004) Biochemistry , vol.43 , pp. 9968-9977
    • Adams, P.D.1    Loh, A.P.2    Oswald, R.E.3
  • 21
    • 34250312793 scopus 로고    scopus 로고
    • 13C assignments for the activated forms of the small Rho-GTPase Rac1
    • 13C assignments for the activated forms of the small Rho-GTPase Rac1. J. Biomol. NMR 36 (2006) 51
    • (2006) J. Biomol. NMR , vol.36 , pp. 51
    • Bouguet-Bonnet, S.1    Buck, M.2
  • 22
    • 0033739987 scopus 로고    scopus 로고
    • The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner
    • Vikis H.G., Li W., He Z., and Guan K.L. The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner. Proc. Natl. Acad. Sci. USA 97 (2000) 12457-12462
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 12457-12462
    • Vikis, H.G.1    Li, W.2    He, Z.3    Guan, K.L.4
  • 23
    • 0035814887 scopus 로고    scopus 로고
    • Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho
    • Driessens M.H., Hu H., Nobes C.D., Self A., Jordens I., Goodman C.S., and Hall A. Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho. Curr. Biol. 11 (2001) 339-344
    • (2001) Curr. Biol. , vol.11 , pp. 339-344
    • Driessens, M.H.1    Hu, H.2    Nobes, C.D.3    Self, A.4    Jordens, I.5    Goodman, C.S.6    Hall, A.7
  • 24
    • 20744434543 scopus 로고    scopus 로고
    • Plexins: axon guidance and signal transduction
    • Negishi M., Oinuma I., and Katoh H. Plexins: axon guidance and signal transduction. Cell Mol. Life Sci. 62 (2005) 1363-1371
    • (2005) Cell Mol. Life Sci. , vol.62 , pp. 1363-1371
    • Negishi, M.1    Oinuma, I.2    Katoh, H.3
  • 25
    • 23144465799 scopus 로고    scopus 로고
    • 13C resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold
    • 13C resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold. J. Biomol. NMR 31 (2005) 369-370
    • (2005) J. Biomol. NMR , vol.31 , pp. 369-370
    • Tong, Y.1    Buck, M.2
  • 26
    • 38949143024 scopus 로고    scopus 로고
    • Insights into oncogenic mutations of plexin-B1 based on the solution structure of the Rho GTPase binding domain
    • Tong Y., Hota P.K., Bagheri Hamaneh M., and Buck M. Insights into oncogenic mutations of plexin-B1 based on the solution structure of the Rho GTPase binding domain. Structure 16 (2008) 246-258
    • (2008) Structure , vol.16 , pp. 246-258
    • Tong, Y.1    Hota, P.K.2    Bagheri Hamaneh, M.3    Buck, M.4
  • 27
    • 37549021146 scopus 로고    scopus 로고
    • Binding of Rac1, Rnd1 and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain
    • Tong Y., Chugha P., Hota P.K., Alviani R.S., Li M., Tempel W., et al. Binding of Rac1, Rnd1 and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain. J. Biol. Chem. 282 (2007) 37215-37224
    • (2007) J. Biol. Chem. , vol.282 , pp. 37215-37224
    • Tong, Y.1    Chugha, P.2    Hota, P.K.3    Alviani, R.S.4    Li, M.5    Tempel, W.6
  • 29
    • 11144219896 scopus 로고    scopus 로고
    • Always look on the bright site of Rho: structural implications for a conserved intermolecular interface
    • Dvorsky R., and Ahmadian M.R. Always look on the bright site of Rho: structural implications for a conserved intermolecular interface. EMBO Rep. 5 (2004) 1130-1136
    • (2004) EMBO Rep. , vol.5 , pp. 1130-1136
    • Dvorsky, R.1    Ahmadian, M.R.2
  • 30
    • 0035659985 scopus 로고    scopus 로고
    • The many faces of Ras: recognition of small GTP-binding proteins
    • Corbett K.D., and Alber T. The many faces of Ras: recognition of small GTP-binding proteins. Trends Biochem. Sci. 26 (2001) 710-716
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 710-716
    • Corbett, K.D.1    Alber, T.2
  • 31
    • 0034687081 scopus 로고    scopus 로고
    • The mechanism of nucleotide release from Rho by the GDP dissociation stimulator protein, GDS
    • Hutchinson J.P., and Eccleston J.F. The mechanism of nucleotide release from Rho by the GDP dissociation stimulator protein, GDS. Biochemistry 39 (2000) 11348-11359
    • (2000) Biochemistry , vol.39 , pp. 11348-11359
    • Hutchinson, J.P.1    Eccleston, J.F.2
  • 32
    • 0026684153 scopus 로고
    • A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems
    • Webb M.R. A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems. Proc. Natl. Acad. Sci. USA 89 (1992) 4884-4887
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4884-4887
    • Webb, M.R.1
  • 33
    • 11844283972 scopus 로고    scopus 로고
    • When monomers are preferred: a strategy for the identification and disruption of weakly oligomerized proteins
    • Tong Y., Hughes D., Placanica L., and Buck M. When monomers are preferred: a strategy for the identification and disruption of weakly oligomerized proteins. Structure 13 (2005) 5-17
    • (2005) Structure , vol.13 , pp. 5-17
    • Tong, Y.1    Hughes, D.2    Placanica, L.3    Buck, M.4
  • 34
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules
    • Lipari G., and Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. J. Am. Chem. Soc. 104 (1982) 4546-4570
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4570
    • Lipari, G.1    Szabo, A.2
  • 37
    • 0031034136 scopus 로고    scopus 로고
    • The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue
    • Hirshberg M., Stockley R.W., Dodson G., and Webb M.R. The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. Nat. Struct. Biol. 4 (1997) 147-152
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 147-152
    • Hirshberg, M.1    Stockley, R.W.2    Dodson, G.3    Webb, M.R.4
  • 40
    • 36849039429 scopus 로고    scopus 로고
    • A hierarchy of timescales in protein dynamics is linked to enzyme catalysis
    • Henzler-Wildman K.A., Lei M., Thai V., Kerns S.J., Karplus M., and Kern D. A hierarchy of timescales in protein dynamics is linked to enzyme catalysis. Nature 450 (2007) 913-916
    • (2007) Nature , vol.450 , pp. 913-916
    • Henzler-Wildman, K.A.1    Lei, M.2    Thai, V.3    Kerns, S.J.4    Karplus, M.5    Kern, D.6
  • 42
    • 0032581920 scopus 로고    scopus 로고
    • Anisotropic intramolecular backbone dynamics of ubiquitin characterized by NMR relaxation and MD computer simulation
    • Lienin S.F., Bremi T., Brutscher B., Bruschweiler R., and Ernst R.R. Anisotropic intramolecular backbone dynamics of ubiquitin characterized by NMR relaxation and MD computer simulation. J. Am. Chem. Soc. 120 (1998) 9870-9879
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 9870-9879
    • Lienin, S.F.1    Bremi, T.2    Brutscher, B.3    Bruschweiler, R.4    Ernst, R.R.5
  • 43
    • 0035937549 scopus 로고    scopus 로고
    • Flipping a switch
    • Buck M., and Rosen M.K. Flipping a switch. Science 291 (2001) 2329-2330
    • (2001) Science , vol.291 , pp. 2329-2330
    • Buck, M.1    Rosen, M.K.2
  • 45
    • 0035901519 scopus 로고    scopus 로고
    • An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs
    • Loh A.P., Pawley N., Nicholson L.K., and Oswald R.E. An increase in side chain entropy facilitates effector binding: NMR characterization of the side chain methyl group dynamics in Cdc42Hs. Biochemistry 40 (2001) 4590-4600
    • (2001) Biochemistry , vol.40 , pp. 4590-4600
    • Loh, A.P.1    Pawley, N.2    Nicholson, L.K.3    Oswald, R.E.4
  • 46
    • 0034760077 scopus 로고    scopus 로고
    • Dynamic activation of protein function: a view emerging from NMR spectroscopy
    • Wand A.J. Dynamic activation of protein function: a view emerging from NMR spectroscopy. Nat. Struct. Biol. 8 (2001) 926-931
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 926-931
    • Wand, A.J.1
  • 47
    • 12144259853 scopus 로고    scopus 로고
    • NMR dynamics derived insights into the binding properties of a peptide interacting with an SH2 domain
    • Finerty P.J., Mittermaier A.K., Muhandiram R., Kay L.E., and Forman-Kay J.D. NMR dynamics derived insights into the binding properties of a peptide interacting with an SH2 domain. Biochemistry 44 (2005) 694-703
    • (2005) Biochemistry , vol.44 , pp. 694-703
    • Finerty, P.J.1    Mittermaier, A.K.2    Muhandiram, R.3    Kay, L.E.4    Forman-Kay, J.D.5
  • 48
    • 33747508183 scopus 로고    scopus 로고
    • Characterization of the backbone and sidechain dynamics of CaM-CaMKIp complex reveals microscopic contributions to protein comformational entropy
    • Frederick K.K., Kranz J.K., and Wand J.A. Characterization of the backbone and sidechain dynamics of CaM-CaMKIp complex reveals microscopic contributions to protein comformational entropy. Biochemistry 45 (2006) 9841-9848
    • (2006) Biochemistry , vol.45 , pp. 9841-9848
    • Frederick, K.K.1    Kranz, J.K.2    Wand, J.A.3
  • 49
    • 0033525126 scopus 로고    scopus 로고
    • Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA
    • Bracken C., Carr P.A., Cavanagh J., and Palmer III A.G. Temperature dependence of intramolecular dynamics of the basic leucine zipper of GCN4: implications for the entropy of association with DNA. J. Mol. Biol. 285 (1999) 2133
    • (1999) J. Mol. Biol. , vol.285 , pp. 2133
    • Bracken, C.1    Carr, P.A.2    Cavanagh, J.3    Palmer III, A.G.4
  • 50
    • 0037407208 scopus 로고    scopus 로고
    • Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling
    • Ferreon J.C., and Hilser V.J. Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling. Protein Sci. 12 (2003) 982
    • (2003) Protein Sci. , vol.12 , pp. 982
    • Ferreon, J.C.1    Hilser, V.J.2
  • 51
    • 20344370764 scopus 로고    scopus 로고
    • Allosteric mechanisms of signal transduction
    • Changeux J.P., and Edelstein S.J. Allosteric mechanisms of signal transduction. Science 308 (2005) 1424-1428
    • (2005) Science , vol.308 , pp. 1424-1428
    • Changeux, J.P.1    Edelstein, S.J.2
  • 52
    • 25444519195 scopus 로고    scopus 로고
    • Backbone and sidechain dynamics of mutant calmodulin-peptide complexes
    • Igumenova T.I., Lee A.L., and Wand A.J. Backbone and sidechain dynamics of mutant calmodulin-peptide complexes. Biochemistry 44 (2005) 12627-12639
    • (2005) Biochemistry , vol.44 , pp. 12627-12639
    • Igumenova, T.I.1    Lee, A.L.2    Wand, A.J.3
  • 53
    • 0035078116 scopus 로고    scopus 로고
    • Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant
    • Evenas J., Malmendal A., and Akke M. Dynamics of the transition between open and closed conformations in a calmodulin C-terminal domain mutant. Structure 9 (2001) 185-195
    • (2001) Structure , vol.9 , pp. 185-195
    • Evenas, J.1    Malmendal, A.2    Akke, M.3
  • 57
    • 0024429207 scopus 로고
    • NMR studies of mobility within protein structure
    • Williams R.J. NMR studies of mobility within protein structure. Eur. J. Biochem. 183 (1989) 479-497
    • (1989) Eur. J. Biochem. , vol.183 , pp. 479-497
    • Williams, R.J.1
  • 58
    • 0034917377 scopus 로고    scopus 로고
    • Physiological conditions and practicality for protein nuclear magnetic resonance spectroscopy: experimental methodologies and theoretical background
    • Kremer W., and Robert H. Physiological conditions and practicality for protein nuclear magnetic resonance spectroscopy: experimental methodologies and theoretical background. Methods Enzymol. 339 (2001) 3-19
    • (2001) Methods Enzymol. , vol.339 , pp. 3-19
    • Kremer, W.1    Robert, H.2
  • 60
    • 33745685964 scopus 로고    scopus 로고
    • Mapping allostery through equilibrium perturbation NMR spectroscopy
    • Das R., Abu-Abed M., and Melacini G. Mapping allostery through equilibrium perturbation NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 8406-8407
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 8406-8407
    • Das, R.1    Abu-Abed, M.2    Melacini, G.3
  • 61
    • 0000477505 scopus 로고    scopus 로고
    • Gifa V4: a complete package for NMR data-set processing
    • Pons J.L., Malliavin T.E., and Delsuc M.A. Gifa V4: a complete package for NMR data-set processing. J. Biomol. NMR 8 (1996) 445-452
    • (1996) J. Biomol. NMR , vol.8 , pp. 445-452
    • Pons, J.L.1    Malliavin, T.E.2    Delsuc, M.A.3
  • 62
    • 0141502348 scopus 로고    scopus 로고
    • Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G
    • Hall J.B., and Fushman D. Characterization of the overall and local dynamics of a protein with intermediate rotational anisotropy: differentiating between conformational exchange and anisotropic diffusion in the B3 domain of protein G. J. Biomol. NMR 27 (2003) 261-275
    • (2003) J. Biomol. NMR , vol.27 , pp. 261-275
    • Hall, J.B.1    Fushman, D.2


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