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Volumn 51, Issue 1-2, 2011, Pages 131-150

Domain cooperativity in multidomain proteins: What can we learn from molecular alignment in anisotropic media?

Author keywords

Alignment tensor; Conformational disorder; Conformational ensemble; Domain domain motion; Electrostatic alignment; Flexible linker; Generalized degree of order; Multidomain proteins; PALES software; PEG hexanol alignment media; Residual dipolar couplings; Steric alignment; Tandem SH3 construct

Indexed keywords

GLYCINE; HEXANOL; MACROGOL; MEMBRANE PROTEIN; PROTEIN SH3; SERINE;

EID: 80755127361     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-011-9548-7     Document Type: Article
Times cited : (18)

References (134)
  • 2
    • 0141747176 scopus 로고    scopus 로고
    • Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings
    • DOI 10.1110/ps.03164403
    • AT Alexandrescu RA Kammerer 2003 Structure and disorder in the ribonuclease S-peptide probed by NMR residual dipolar couplings Protein Sci 12 2132 2140 10.1110/ps.03164403 (Pubitemid 37163348)
    • (2003) Protein Science , vol.12 , Issue.10 , pp. 2132-2140
    • Alexandrescu, A.T.1    Kammerer, R.A.2
  • 3
    • 37549044716 scopus 로고    scopus 로고
    • 13C NMR spectroscopy: Application to apo calmodulin
    • 10.1021/ja0721824
    • 13C NMR spectroscopy: Application to apo calmodulin J Am Chem Soc 129 15805 15813 10.1021/ja0721824
    • (2007) J Am Chem Soc , vol.129 , pp. 15805-15813
    • Andre, I.1    Linse, S.2    Mulder, F.A.A.3
  • 4
    • 33745473771 scopus 로고    scopus 로고
    • Molecular ordering and structure of quasi-spherical solutes by liquid crystal NMR and Monte Carlo simulations: The case of norbornadiene
    • DOI 10.1021/jp061345s
    • C Aroulanda G Celebre G De Luca M Longeri 2006 Molecular ordering and structure of quasi-spherical solutes by liquid crystal NMR and Monte Carlo simulations: the case of norbornadiene J Phys Chem B 110 10485 10496 10.1021/jp061345s (Pubitemid 43952944)
    • (2006) Journal of Physical Chemistry B , vol.110 , Issue.21 , pp. 10485-10496
    • Aroulanda, C.1    Celebre, G.2    De Luca, G.3    Longeri, M.4
  • 5
    • 67650529516 scopus 로고    scopus 로고
    • Prediction of the rotational tumbling time for proteins with disordered segments
    • 10.1021/ja809687r
    • SH Bae HJ Dyson PE Wright 2009 Prediction of the rotational tumbling time for proteins with disordered segments J Am Chem Soc 131 6814 6821 10.1021/ja809687r
    • (2009) J Am Chem Soc , vol.131 , pp. 6814-6821
    • Bae, S.H.1    Dyson, H.J.2    Wright, P.E.3
  • 6
    • 0027888184 scopus 로고
    • Cloud point phenomena in the phase behavior of alkyl polyglucosides in water
    • 10.1021/la00036a009
    • D Balzer 1993 Cloud point phenomena in the phase behavior of alkyl polyglucosides in water Langmuir 9 3375 3384 10.1021/la00036a009
    • (1993) Langmuir , vol.9 , pp. 3375-3384
    • Balzer, D.1
  • 8
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • DOI 10.1110/ps.0233303
    • A Bax 2003 Weak alignment offers new NMR opportunities to study protein structure and dynamics Protein Sci 12 1 16 10.1110/ps.0233303 (Pubitemid 36020129)
    • (2003) Protein Science , vol.12 , Issue.1 , pp. 1-16
    • Bax, A.1
  • 9
    • 0031244139 scopus 로고    scopus 로고
    • High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium
    • A Bax N Tjandra 1997 High-resolution heteronuclear NMR of human ubiquitin in an aqueous liquid crystalline medium J Biomol NMR 10 289 292 10.1023/A:1018308717741 (Pubitemid 127504676)
    • (1997) Journal of Biomolecular NMR , vol.10 , Issue.3 , pp. 289-292
    • Bax, A.1    Tjandra, N.2
  • 10
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • DOI 10.1016/S0076-6879(01)39313-8
    • A Bax G Kontaxis N Tjandra 2001 Dipolar couplings in macromolecular structure determination Method Enzymol 339 127 174 10.1016/S0076-6879(01)39313-8 (Pubitemid 32666560)
    • (2001) Methods in Enzymology , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 11
    • 70349748272 scopus 로고    scopus 로고
    • Improvement and analysis of computational methods for prediction of residual dipolar couplings
    • 2009JMagR.201.25B 10.1016/j.jmr.2009.07.028
    • K Berlin DP O'Leary D Fushman 2009 Improvement and analysis of computational methods for prediction of residual dipolar couplings J Magn Reson 201 25 33 2009JMagR.201...25B 10.1016/j.jmr.2009.07.028
    • (2009) J Magn Reson , vol.201 , pp. 25-33
    • Berlin, K.1    O'Leary, D.P.2    Fushman, D.3
  • 14
    • 35548988910 scopus 로고    scopus 로고
    • Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains
    • DOI 10.1021/ja0726613
    • I Bertini YK Gupta C Luchinat G Parigi M Peana L Sgheri J Yuan 2007 Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains J Am Chem Soc 129 12786 12794 10.1021/ja0726613 (Pubitemid 350004491)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.42 , pp. 12786-12794
    • Bertini, I.1    Gupta, Y.K.2    Luchinat, C.3    Parigi, G.4    Peana, M.5    Sgheri, L.6    Yuan, J.7
  • 15
    • 0034791996 scopus 로고    scopus 로고
    • Solution structure of a cyanovirin-N:Manα1-2Manα complex: Structural basis for high-affinity carbohydrate-mediated binding to gp120
    • DOI 10.1016/S0969-2126(01)00653-0, PII S0969212601006530
    • Bewley CA (2001) Solution structure of a cyanovirin-N: Manα1-2Manα complex: structural basis for high-affinity carbohydrate-mediated binding to gp120. Structure 9:931-940 (Pubitemid 32972159)
    • (2001) Structure , vol.9 , Issue.10 , pp. 931-940
    • Bewley, C.A.1
  • 16
    • 0031160370 scopus 로고    scopus 로고
    • 15N NMR assignment and solution structure of the SH3 domain of spectrin: Comparison of unrefined and refined structure sets with the crystal structure
    • 15N NMR assignment and solution structure of the SH3 domain of spectrin: comparison of unrefined and refined structure sets with the crystal structure J Biomol NMR 9 347 357 10.1023/A:1018330122908 (Pubitemid 127505397)
    • (1997) Journal of Biomolecular NMR , vol.9 , Issue.4 , pp. 347-357
    • Blanco, F.J.1    Ortiz, A.R.2    Serrano, L.3
  • 17
    • 0035812416 scopus 로고    scopus 로고
    • Rapid identification of medium- to large-scale interdomain motion in modular proteins using dipolar couplings [21]
    • DOI 10.1021/ja016234f
    • DT Braddock ML Cai JL Baber Y Huang GM Clore 2001 Rapid identification of medium- to large-scale interdomain motion in modular proteins using dipolar couplings J Am Chem Soc 123 8634 8635 10.1021/ja016234f (Pubitemid 32808100)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.35 , pp. 8634-8635
    • Braddock, D.T.1    Cai, M.2    Baber, J.L.3    Huang, Y.4    Clore, G.M.5
  • 18
    • 0036646504 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: Solution structure of a complex between hnRNP K KH3 and single-stranded DNA
    • DOI 10.1093/emboj/cdf352
    • DT Braddock JL Baber D Levens GM Clore 2002 Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP KKH3 and single-stranded DNA EMBO J 21 3476 3485 10.1093/emboj/cdf352 (Pubitemid 34760579)
    • (2002) EMBO Journal , vol.21 , Issue.13 , pp. 3476-3485
    • Braddock, D.T.1    Baber, J.L.2    Levens, D.3    Clore, G.M.4
  • 19
    • 0042933782 scopus 로고    scopus 로고
    • De novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracy
    • DOI 10.1021/ja035904+
    • KB Briggman JR Tolman 2003 De Novo determination of bond orientations and order parameters from residual dipolar couplings with high accuracy J Am Chem Soc 125 10164 10165 10.1021/ja035904+ (Pubitemid 37022214)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.34 , pp. 10164-10165
    • Briggman, K.B.1    Tolman, J.R.2
  • 21
    • 69949128980 scopus 로고    scopus 로고
    • NMR analysis of the architecture and functional remodeling of a modular multidomain protein, RPA
    • 10.1021/ja9013634
    • CA Brosey ME Chagot M Ehrhardt DI Pretto BE Weiner WJ Chazin 2009 NMR analysis of the architecture and functional remodeling of a modular multidomain protein, RPA J Am Chem Soc 131 6346 6347 10.1021/ja9013634
    • (2009) J Am Chem Soc , vol.131 , pp. 6346-6347
    • Brosey, C.A.1    Chagot, M.E.2    Ehrhardt, M.3    Pretto, D.I.4    Weiner, B.E.5    Chazin, W.J.6
  • 22
    • 0023449962 scopus 로고
    • Spin glasses and the statistical mechanics of protein folding
    • 1987PNAS.84.7524B 10.1073/pnas.84.21.7524
    • JD Bryngelson PG Wolynes 1987 Spin glasses and the statistical mechanics of protein folding Proc Natl Acad Sci USA 84 7524 7528 1987PNAS...84.7524B 10.1073/pnas.84.21.7524
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7524-7528
    • Bryngelson, J.D.1    Wolynes, P.G.2
  • 23
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • 10.1002/prot.340210302
    • JD Bryngelson JN Onuchic ND Socci PG Wolynes 1995 Funnels, pathways, and the energy landscape of protein folding: a synthesis Proteins Struct Funct Genet 21 167 195 10.1002/prot.340210302
    • (1995) Proteins Struct Funct Genet , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 24
    • 24944446722 scopus 로고    scopus 로고
    • G. Cesareni M. Gimona M. Sudol M. Yaffe (eds). Wiley-VCH Weinheim
    • Cesareni G, Gimona M, Sudol M, Yaffe M (eds) (2005) Modular protein domains. Wiley-VCH, Weinheim
    • (2005) Modular Protein Domains
  • 25
    • 52449112128 scopus 로고    scopus 로고
    • Extended model free approach to analyze correlation functions of multidomain proteins in the presence of motional coupling
    • 10.1021/ja803557t
    • K Chen N Tjandra 2008 Extended model free approach to analyze correlation functions of multidomain proteins in the presence of motional coupling J Am Chem Soc 130 12745 12751 10.1021/ja803557t
    • (2008) J Am Chem Soc , vol.130 , pp. 12745-12751
    • Chen, K.1    Tjandra, N.2
  • 26
    • 23844547333 scopus 로고    scopus 로고
    • Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of α-spectrin by MAS solid-state NMR
    • DOI 10.1007/s10858-005-1718-z
    • V Chevelkov K Faelber A Diehl U Heinemann H Oschkinat B Reif 2005 Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of α-spectrin by MAS solid-state NMR J Biomol NMR 31 295 310 10.1007/s10858-005-1718-z (Pubitemid 41348906)
    • (2005) Journal of Biomolecular NMR , vol.31 , Issue.4 , pp. 295-310
    • Chevelkov, V.1    Faelber, K.2    Diehl, A.3    Heinemann, U.4    Oschkinat, H.5    Reif, B.6
  • 28
    • 77950817927 scopus 로고    scopus 로고
    • Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics
    • 10.1021/ja100645k
    • V Chevelkov Y Xue R Linser NR Skrynnikov B Reif 2010 Comparison of solid-state dipolar couplings and solution relaxation data provides insight into protein backbone dynamics J Am Chem Soc 132 5015 5017 10.1021/ja100645k
    • (2010) J Am Chem Soc , vol.132 , pp. 5015-5017
    • Chevelkov, V.1    Xue, Y.2    Linser, R.3    Skrynnikov, N.R.4    Reif, B.5
  • 29
    • 34250663523 scopus 로고    scopus 로고
    • Abl functions as a negative regulator of Met-induced cell motility via phosphorylation of the adapter protein CrkII
    • DOI 10.1016/j.cellsig.2007.02.011, PII S0898656807000757
    • A Cipres YA Abassi K Vuori 2007 Abl functions as a negative regulator of Met-induced cell motility via phosphorylation of the adapter protein CrkII Cell Signal 19 1662 1670 10.1016/j.cellsig.2007.02.011 (Pubitemid 46935423)
    • (2007) Cellular Signalling , vol.19 , Issue.8 , pp. 1662-1670
    • Cipres, A.1    Abassi, Y.A.2    Vuori, K.3
  • 30
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • DOI 10.1021/ja9812610
    • G Cornilescu JL Marquardt M Ottiger A Bax 1998 Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase J Am Chem Soc 120 6836 6837 10.1021/ja9812610 (Pubitemid 28347351)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.27 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 31
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • JG de la Torre ML Huertas B Carrasco 2000 Calculation of hydrodynamic properties of globular proteins from their atomic-level structure Biophys J 78 719 730 10.1016/S0006-3495(00)76630-6 (Pubitemid 30211830)
    • (2000) Biophysical Journal , vol.78 , Issue.2 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 32
    • 0029400480 scopus 로고
    • NMRPipe-a multidimensional spectral processing system based on unix pipes
    • 10.1007/BF00197809
    • F Delaglio S Grzesiek GW Vuister G Zhu J Pfeifer A Bax 1995 NMRPipe-a multidimensional spectral processing system based on unix pipes J Biomol NMR 6 277 293 10.1007/BF00197809
    • (1995) J Biomol NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 33
    • 77954759927 scopus 로고    scopus 로고
    • Protein alignment using cellulose nanocrystals: Practical considerations and range of application
    • 10.1007/s10858-010-9423-y
    • AY Denisov E Kloser DG Gray AK Mittermaier 2010 Protein alignment using cellulose nanocrystals: practical considerations and range of application J Biomol NMR 47 195 204 10.1007/s10858-010-9423-y
    • (2010) J Biomol NMR , vol.47 , pp. 195-204
    • Denisov, A.Y.1    Kloser, E.2    Gray, D.G.3    Mittermaier, A.K.4
  • 34
    • 0038637840 scopus 로고    scopus 로고
    • Ordering of apolar and polar solutes in nematic solvents
    • 2003JChPh.118.7046D 10.1063/1.1560941
    • T Dingemans DJ Photinos ET Samulski AF Terzis C Wutz 2003 Ordering of apolar and polar solutes in nematic solvents J Chem Phys 118 7046 7061 2003JChPh.118.7046D 10.1063/1.1560941
    • (2003) J Chem Phys , vol.118 , pp. 7046-7061
    • Dingemans, T.1    Photinos, D.J.2    Samulski, E.T.3    Terzis, A.F.4    Wutz, C.5
  • 35
    • 84961985307 scopus 로고    scopus 로고
    • Development of a generalized born model parametrization for proteins and nucleic acids
    • BN Dominy CL Brooks 1999 Development of a generalized Born model parametrization for proteins and nucleic acids J Phys Chem B 103 3765 3773 10.1021/jp984440c (Pubitemid 129702431)
    • (1999) Journal of Physical Chemistry B , vol.103 , Issue.18 , pp. 3765-3773
    • Dominy, B.N.1    Brooks III, C.L.2
  • 37
    • 0015000566 scopus 로고
    • Stabilization of oil-in-water emulsions by nonionic detergents. 5. Effect of salts on rates of coalescence in a chlorobenzene emulsion
    • 10.1016/0021-9797(71)90180-9
    • PH Elworthy JA Rogers AT Florence 1971 Stabilization of oil-in-water emulsions by nonionic detergents. 5. Effect of salts on rates of coalescence in a chlorobenzene emulsion J Colloid Interf Sci 35 23 33 10.1016/0021-9797(71) 90180-9
    • (1971) J Colloid Interf Sci , vol.35 , pp. 23-33
    • Elworthy, P.H.1    Rogers, J.A.2    Florence, A.T.3
  • 38
    • 0000333343 scopus 로고
    • The inclusion of electrostatic and dispersion interactions into potentials of mean torque for solutes dissolved in uniaxial liquid-crystal solvents
    • 10.1080/02678299108030378
    • JW Emsley WE Palke GN Shilstone 1991 The inclusion of electrostatic and dispersion interactions into potentials of mean torque for solutes dissolved in uniaxial liquid-crystal solvents Liq Cryst 9 643 648 10.1080/02678299108030378
    • (1991) Liq Cryst , vol.9 , pp. 643-648
    • Emsley, J.W.1    Palke, W.E.2    Shilstone, G.N.3
  • 39
    • 0034193509 scopus 로고    scopus 로고
    • A fast method to sample real protein conformational space
    • DOI 10.1002/(SICI)1097-0134(20000501)39:2<112::AID-PROT2>3.0.CO;2-B
    • HJ Feldman CWV Hogue 2000 A fast method to sample real protein conformational space Proteins Struct Funct Genet 39 112 131 10.1002/(SICI)1097- 0134(20000501)39:2<112::AID-PROT2>3.0.CO;2-B (Pubitemid 30176479)
    • (2000) Proteins: Structure, Function and Genetics , vol.39 , Issue.2 , pp. 112-131
    • Feldman, H.J.1    Hogue, C.W.V.2
  • 40
    • 0035475308 scopus 로고    scopus 로고
    • CrK family adaptors-signalling complex formation and biological roles
    • DOI 10.1038/sj.onc.1204779
    • SM Feller 2001 Crk family adaptors-signalling complex formation and biological roles Oncogene 20 6348 6371 10.1038/sj.onc.1204779 (Pubitemid 32977844)
    • (2001) Oncogene , vol.20 , pp. 6348-6371
    • Feller, S.M.1
  • 41
    • 27244458959 scopus 로고    scopus 로고
    • NMR spectroscopic characterization of the membrane affinity of polyols
    • DOI 10.1002/mrc.1653
    • D Fischer A Geyer 2005 NMR spectroscopic characterization of the membrane affinity of polyols Magn Reson Chem 43 893 901 10.1002/mrc.1653 (Pubitemid 41512843)
    • (2005) Magnetic Resonance in Chemistry , vol.43 , Issue.11 , pp. 893-901
    • Fischer, D.1    Geyer, A.2
  • 44
    • 0032555744 scopus 로고    scopus 로고
    • Structural basis for Syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide
    • DOI 10.1006/jmbi.1998.1964
    • K Futterer J Wong RA Grucza AC Chan G Waksman 1998 Structural basis for syk tyrosine kinase ubiquity in signal transduction pathways revealed by the crystal structure of its regulatory SH2 domains bound to a dually phosphorylated ITAM peptide J Mol Biol 281 523 537 10.1006/jmbi.1998.1964 (Pubitemid 28372129)
    • (1998) Journal of Molecular Biology , vol.281 , Issue.3 , pp. 523-537
    • Futterer, K.1    Wong, J.2    Grucza, R.A.3    Chan, A.C.4    Waksman, G.5
  • 45
    • 0035852133 scopus 로고    scopus 로고
    • Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy
    • DOI 10.1021/ja011967l
    • S Gaemers A Bax 2001 Morphology of three lyotropic liquid crystalline biological NMR media studied by translational diffusion anisotropy J Am Chem Soc 123 12343 12352 10.1021/ja011967l (Pubitemid 33136071)
    • (2001) Journal of the American Chemical Society , vol.123 , Issue.49 , pp. 12343-12352
    • Gaemers, S.1    Bax, A.2
  • 46
    • 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 AMJJ Bonvin D Keramisanou M Koukaki G Gouridis S Karamanou A Economou CG Kalodimos 2007 Structural basis for signal-sequence recognition by the translocase motor SecA as determined by NMR Cell 131 756 769 10.1016/j.cell.2007.09.039 (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
  • 48
    • 73349129075 scopus 로고    scopus 로고
    • The structure of Mg-ATPase nucleotide-binding domain at 1.6 angstrom resolution reveals a unique ATP-binding motif
    • 10.1107/S090744490903306X
    • KO Hakansson 2009 The structure of Mg-ATPase nucleotide-binding domain at 1.6 angstrom resolution reveals a unique ATP-binding motif Acta Crystallogr D 65 1181 1186 10.1107/S090744490903306X
    • (2009) Acta Crystallogr D , vol.65 , pp. 1181-1186
    • Hakansson, K.O.1
  • 49
    • 65649138745 scopus 로고    scopus 로고
    • 1H, 13C and 15 N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19
    • 10.1007/s12104-008-9140-6
    • O Heikkinen P Permi H Koskela J Ylanne I Kilpelainen 2009 1H, 13C and 15 N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19 Biomol NMR Assign 3 53 56 10.1007/s12104-008-9140-6
    • (2009) Biomol NMR Assign , vol.3 , pp. 53-56
    • Heikkinen, O.1    Permi, P.2    Koskela, H.3    Ylanne, J.4    Kilpelainen, I.5
  • 50
    • 44449120062 scopus 로고    scopus 로고
    • Two domains of RD3 antifreeze protein diffuse independently
    • DOI 10.1021/bi8001924
    • NB Holland Y Nishimiya S Tsuda FD Sonnichsen 2008 Two domains of RD3 antifreeze protein diffuse independently Biochemistry 47 5935 5941 10.1021/bi8001924 (Pubitemid 351770023)
    • (2008) Biochemistry , vol.47 , Issue.22 , pp. 5935-5941
    • Holland, N.B.1    Nishimiya, Y.2    Tsuda, S.3    Sonnichsen, F.D.4
  • 52
    • 3042724646 scopus 로고    scopus 로고
    • Novel techniques for weak alignment of proteins in solution using chemical tags coordinating lanthanide ions
    • DOI 10.1023/B:JNMR.0000032611.72827.de
    • T Ikegami L Verdier P Sakhaii S Grimme B Pescatore K Saxena KM Fiebig C Griesinger 2004 Novel techniques for weak alignment of proteins in solution using chemical tags coordinating lanthanide ions J Biomol NMR 29 339 349 10.1023/B:JNMR.0000032611.72827.de (Pubitemid 38864832)
    • (2004) Journal of Biomolecular NMR , vol.29 , Issue.3 , pp. 339-349
    • Ikegami, T.1    Verdier, L.2    Sakhaii, P.3    Grimme, S.4    Pescatore, B.5    Saxena, K.6    Fiebig, K.M.7    Griesinger, C.8
  • 53
    • 0025866660 scopus 로고
    • Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle Myosin Light-Chain Kinase: Indication of a conformational change in the central helix
    • 10.1021/bi00236a024
    • M Ikura LE Kay M Krinks A Bax 1991 Triple-resonance multidimensional NMR study of calmodulin complexed with the binding domain of skeletal muscle Myosin Light-Chain Kinase: indication of a conformational change in the central helix Biochemistry 30 5498 5504 10.1021/bi00236a024
    • (1991) Biochemistry , vol.30 , pp. 5498-5504
    • Ikura, M.1    Kay, L.E.2    Krinks, M.3    Bax, A.4
  • 54
    • 45749102885 scopus 로고    scopus 로고
    • Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: Application to the molecular recognition element of Sendai virus nucleoprotein
    • DOI 10.1021/ja801332d
    • MR Jensen K Houben E Lescop L Blanchard RWH Ruigrok M Blackledge 2008 Quantitative conformational analysis of partially folded proteins from residual dipolar couplings: Application to the molecular recognition element of Sendai virus nucleoprotein J Am Chem Soc 130 8055 8061 10.1021/ja801332d (Pubitemid 351875082)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.25 , pp. 8055-8061
    • Jensen, M.R.1    Houben, K.2    Lescop, E.3    Blanchard, L.4    Ruigrok, R.W.H.5    Blackledge, M.6
  • 55
    • 0026122420 scopus 로고
    • Protein surface interactions in the presence of polyethylene oxide. I. Simplified theory
    • 10.1016/0021-9797(91)90043-8
    • SI Jeon JH Lee JD Andrade PG De Gennes 1991 Protein surface interactions in the presence of polyethylene oxide. I. Simplified theory J Colloid Interf Sci 142 149 158 10.1016/0021-9797(91)90043-8
    • (1991) J Colloid Interf Sci , vol.142 , pp. 149-158
    • Jeon, S.I.1    Lee, J.H.2    Andrade, J.D.3    De Gennes, P.G.4
  • 56
    • 26744472420 scopus 로고
    • Nonionic bilayers in dilute solutions: Effect of additives
    • 10.1021/j100193a064
    • M Jonstromer R Strey 1992 Nonionic bilayers in dilute solutions: effect of additives J Phys Chem 96 5993 6000 10.1021/j100193a064
    • (1992) J Phys Chem , vol.96 , pp. 5993-6000
    • Jonstromer, M.1    Strey, R.2
  • 57
    • 77950463927 scopus 로고    scopus 로고
    • Chitobiose complex of the N,N'-diacetylchitobiose branch of the Escherichia Coli phosphotransferase system
    • Chitobiose complex of the N,N'-diacetylchitobiose branch of the Escherichia Coli phosphotransferase system. J Biol Chem 285:4173-4184
    • (2010) J Biol Chem , vol.285 , pp. 4173-4184
    • Jung, Y.S.1    Cai, M.L.2    Clore, G.M.3
  • 58
    • 0037169896 scopus 로고    scopus 로고
    • Disjoining pressures, zeta potentials and surface tensions of aqueous non-ionic surfactant/electrolyte solutions: Theory and comparison to experiment
    • DOI 10.1016/S0001-8686(01)00083-5, PII S0001868601000835
    • KA Karraker CJ Radke 2002 Disjoining pressures zeta potentials and surface tensions of aqueous non-ionic surfactant/electrolyte solutions: theory and comparison to experiment Adv Colloid Interfac 96 231 264 10.1016/S0001-8686(01)00083-5 (Pubitemid 34154689)
    • (2002) Advances in Colloid and Interface Science , vol.96 , Issue.1-3 , pp. 231-264
    • Karraker, K.A.1    Radke, C.J.2
  • 59
    • 34547657260 scopus 로고    scopus 로고
    • Increased paramagnetic effect of a lanthanide protein probe by two-point attachment
    • DOI 10.1021/ja0725201
    • PHJ Keizers JF Desreux M Overhand M Ubbink 2007 Increased paramagnetic effect of a lanthanide protein probe by two-point attachment J Am Chem Soc 129 9292 9293 10.1021/ja0725201 (Pubitemid 47218791)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.30 , pp. 9292-9293
    • Keizers, P.H.J.1    Desreux, J.F.2    Overhand, M.3    Ubbink, M.4
  • 60
    • 33747131772 scopus 로고    scopus 로고
    • Toward the accurate first-principles prediction of ionization equilibria in proteins
    • DOI 10.1021/bi060706r
    • J Khandogin CL Brooks 2006 Toward the accurate first-principles prediction of ionization equilibria in proteins Biochemistry 45 9363 9373 10.1021/bi060706r (Pubitemid 44223241)
    • (2006) Biochemistry , vol.45 , Issue.31 , pp. 9363-9373
    • Khandogin, J.1    Brooks III, C.L.2
  • 62
    • 0033577017 scopus 로고    scopus 로고
    • NMR measurement of dipolar couplings in proteins aligned by transient binding to purple membrane fragments [4]
    • DOI 10.1021/ja9837856
    • BW Koenig JS Hu M Ottiger S Bose RW Hendler A Bax 1999 NMR measurement of dipolar couplings in proteins aligned by transient binding to purple membrane fragments J Am Chem Soc 121 1385 1386 10.1021/ja9837856 (Pubitemid 29104071)
    • (1999) Journal of the American Chemical Society , vol.121 , Issue.6 , pp. 1385-1386
    • Koenig, B.W.1    Hu, J.-S.2    Ottiger, M.3    Bose, S.4    Hendler, R.W.5    Bax, A.6
  • 63
    • 77956501272 scopus 로고    scopus 로고
    • A transient and low-populated protein-folding intermediate at atomic resolution
    • 2010Sci.329.1312K 10.1126/science.1191723
    • DM Korzhnev TL Religa W Banachewicz AR Fersht LE Kay 2010 A transient and low-populated protein-folding intermediate at atomic resolution Science 329 1312 1316 2010Sci...329.1312K 10.1126/science.1191723
    • (2010) Science , vol.329 , pp. 1312-1316
    • Korzhnev, D.M.1    Religa, T.L.2    Banachewicz, W.3    Fersht, A.R.4    Kay, L.E.5
  • 64
    • 33645469988 scopus 로고    scopus 로고
    • A thorough dynamic interpretation of residual dipolar couplings in ubiquitin
    • 10.1007/s10858-005-5686-0
    • NA Lakomek T Carlomagno S Becker C Griesinger J Meiler 2006 A thorough dynamic interpretation of residual dipolar couplings in ubiquitin J Biomol NMR 34 101 115 10.1007/s10858-005-5686-0
    • (2006) J Biomol NMR , vol.34 , pp. 101-115
    • Lakomek, N.A.1    Carlomagno, T.2    Becker, S.3    Griesinger, C.4    Meiler, J.5
  • 65
    • 0030992890 scopus 로고    scopus 로고
    • De novo design of the hydrophobic core of ubiquitin
    • GA Lazar JR Desjarlais TM Handel 1997 De novo design of the hydrophobic core of ubiquitin Protein Sci 6 1167 1178 10.1002/pro.5560060605 (Pubitemid 27260151)
    • (1997) Protein Science , vol.6 , Issue.6 , pp. 1167-1178
    • Lazar, G.A.1    Desjarlais, J.R.2    Handel, T.M.3
  • 68
    • 33745135776 scopus 로고    scopus 로고
    • Involvement of adaptor protein Crk in malignant feature of human ovarian cancer cell line MCAS
    • DOI 10.1038/sj.onc.1209398, PII 1209398
    • H Linghu M Tsuda Y Makino M Sakai T Watanabe S Ichihara H Sawa K Nagashima N Mochizuki S Tanaka 2006 Involvement of adaptor protein Crk in malignant feature of human ovarian cancer cell line MCAS Oncogene 25 3547 3556 10.1038/sj.onc.1209398 (Pubitemid 43901676)
    • (2006) Oncogene , vol.25 , Issue.25 , pp. 3547-3556
    • Linghu, H.1    Tsuda, M.2    Makino, Y.3    Sakai, M.4    Watanabe, T.5    Ichihara, S.6    Sawa, H.7    Nagashima, K.8    Mochizuki, N.9    Tanaka, S.10
  • 69
    • 53249115359 scopus 로고    scopus 로고
    • Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution
    • 10.1021/bi800843c
    • AS Maltsev AH Ahmed MK Fenwick DE Jane RE Oswald 2008 Mechanism of partial agonism at the GluR2 AMPA receptor: Measurements of lobe orientation in solution Biochemistry 47 10600 10610 10.1021/bi800843c
    • (2008) Biochemistry , vol.47 , pp. 10600-10610
    • Maltsev, A.S.1    Ahmed, A.H.2    Fenwick, M.K.3    Jane, D.E.4    Oswald, R.E.5
  • 70
    • 0031825181 scopus 로고    scopus 로고
    • Obligatory steps in protein folding and the conformational diversity of the transition state
    • DOI 10.1038/1418
    • JC Martinez MT Pisabarro L Serrano 1998 Obligatory steps in protein folding and the conformational diversity of the transition state Nat Struct Biol 5 721 729 10.1038/1418 (Pubitemid 28359809)
    • (1998) Nature Structural Biology , vol.5 , Issue.8 , pp. 721-729
    • Martinez, J.C.1    Pisabarro, M.T.2    Serrano, L.3
  • 71
    • 0032488495 scopus 로고    scopus 로고
    • Prevention of protein adsorption by tethered poly(ethylene oxide) layers: Experiments and single-chain mean-field analysis
    • T McPherson A Kidane I Szleifer K Park 1998 Prevention of protein adsorption by tethered poly(ethylene oxide) layers: experiments and single-chain mean-field analysis Langmuir 14 176 186 10.1021/la9706781 (Pubitemid 128575461)
    • (1998) Langmuir , vol.14 , Issue.1 , pp. 176-186
    • McPherson, T.1    Kidane, A.2    Szleifer, I.3    Park, K.4
  • 73
    • 3242789489 scopus 로고    scopus 로고
    • Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings
    • DOI 10.1016/j.jmb.2004.05.022, PII S0022283604005881
    • R Mohana-Borges NK Goto GJA Kroon HJ Dyson PE Wright 2004 Structural characterization of unfolded states of apomyoglobin using residual dipolar couplings J Mol Biol 340 1131 1142 10.1016/j.jmb.2004.05.022 (Pubitemid 38968706)
    • (2004) Journal of Molecular Biology , vol.340 , Issue.5 , pp. 1131-1142
    • Mohana-Borges, R.1    Goto, N.K.2    Kroon, G.J.A.3    Dyson, H.J.4    Wright, P.E.5
  • 74
    • 0032866940 scopus 로고    scopus 로고
    • Structural constraints from residual tensorial couplings in high resolution NMR without an explicit term for the alignment tensor
    • DOI 10.1023/A:1008309630377
    • S Moltke S Grzesiek 1999 Structural constraints from residual tensorial couplings in high resolution NMR without an explicit term for the alignment tensor J Biomol NMR 15 77 82 10.1023/A:1008309630377 (Pubitemid 29488031)
    • (1999) Journal of Biomolecular NMR , vol.15 , Issue.1 , pp. 77-82
    • Moltke, S.1    Grzesiek, S.2
  • 76
    • 33746220057 scopus 로고    scopus 로고
    • Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II
    • DOI 10.1021/bi060590z
    • V Muralidharan K Dutta J Cho M Vila-Perello DP Raleigh D Cowburn TW Muir 2006 Solution structure and folding characteristics of the C-terminal SH3 domain of c-Crk-II Biochemistry 45 8874 8884 10.1021/bi060590z (Pubitemid 44100683)
    • (2006) Biochemistry , vol.45 , Issue.29 , pp. 8874-8884
    • Muralidharan, V.1    Dutta, K.2    Cho, J.3    Vila-Perello, M.4    Raleigh, D.P.5    Cowburn, D.6    Muir, T.W.7
  • 77
    • 0026437577 scopus 로고
    • Crystal structure of a Src-homology 3 (SH3) domain
    • 1992Natur.359.851M 10.1038/359851a0
    • A Musacchio M Noble R Pauptit R Wierenga M Saraste 1992 Crystal structure of a Src-homology 3 (SH3) domain Nature 359 851 855 1992Natur.359..851M 10.1038/359851a0
    • (1992) Nature , vol.359 , pp. 851-855
    • Musacchio, A.1    Noble, M.2    Pauptit, R.3    Wierenga, R.4    Saraste, M.5
  • 79
    • 0028335709 scopus 로고
    • The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells
    • S Ogawa H Toyoshima H Kozutsumi K Hagiwara R Sakai T Tanaka N Hirano H Mano Y Yazaki H Hirai 1994 The C-Terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine phosphorylation of Crk associated p130 in rat 3Y1 cells Oncogene 9 1669 1678 (Pubitemid 24163394)
    • (1994) Oncogene , vol.9 , Issue.6 , pp. 1669-1678
    • Ogawa, S.1    Toyoshima, H.2    Kozutsumi, H.3    Hagiwara, K.4    Sakai, R.5    Tanaka, T.6    Hirano, N.7    Mano, H.8    Yazaki, Y.9    Hirai, H.10
  • 80
    • 0037340833 scopus 로고    scopus 로고
    • Observation of residual dipolar couplings in short peptides
    • DOI 10.1002/prot.10327
    • S Ohnishi D Shortle 2003 Observation of residual dipolar couplings in short peptides Proteins Struct Funct Genet 50 546 551 10.1002/prot.10327 (Pubitemid 36330478)
    • (2003) Proteins: Structure, Function and Genetics , vol.50 , Issue.4 , pp. 546-551
    • Ohnishi, S.1    Shortle, D.2
  • 81
    • 38449121914 scopus 로고    scopus 로고
    • Bicelle samples for solid-state NMR of membrane proteins
    • 10.1038/nprot.2007.329
    • SJ Opella AA De Angelis 2007 Bicelle samples for solid-state NMR of membrane proteins Nat Protoc 2 2332 2338 10.1038/nprot.2007.329
    • (2007) Nat Protoc , vol.2 , pp. 2332-2338
    • Opella, S.J.1    De Angelis, A.A.2
  • 82
    • 0032174883 scopus 로고    scopus 로고
    • Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules
    • M Ottiger A Bax 1998 Characterization of magnetically oriented phospholipid micelles for measurement of dipolar couplings in macromolecules J Biomol NMR 12 361 372 10.1023/A:1008366116644 (Pubitemid 128511302)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.3 , pp. 361-372
    • Ottiger, M.1    Bax, A.2
  • 83
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and Dipolar Couplings from Simplified Two-Dimensional NMR Spectra
    • M Ottiger F Delaglio A Bax 1998 Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra J Magn Reson 131 373 378 1998JMagR.131..373O 10.1006/jmre.1998.1361 (Pubitemid 128450579)
    • (1998) Journal of Magnetic Resonance , vol.131 , Issue.2 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 84
    • 53349164086 scopus 로고    scopus 로고
    • Inhibitory receptor signaling via tyrosine phosphorylation of the adaptor Crk
    • 10.1016/j.immuni.2008.07.014
    • ME Peterson EO Long 2008 Inhibitory receptor signaling via tyrosine phosphorylation of the adaptor Crk Immunity 29 578 588 10.1016/j.immuni.2008.07. 014
    • (2008) Immunity , vol.29 , pp. 578-588
    • Peterson, M.E.1    Long, E.O.2
  • 85
    • 78650995206 scopus 로고    scopus 로고
    • Structural Signature of the MYPT1-PP1 Interaction
    • 10.1021/ja107810r
    • AS Pinheiro JA Marsh JD Forman-Kay W Peti 2011 Structural Signature of the MYPT1-PP1 Interaction J Am Chem Soc 133 73 80 10.1021/ja107810r
    • (2011) J Am Chem Soc , vol.133 , pp. 73-80
    • Pinheiro, A.S.1    Marsh, J.A.2    Forman-Kay, J.D.3    Peti, W.4
  • 86
    • 23844517491 scopus 로고    scopus 로고
    • Role of lipid charge in organization of water/lipid bilayer interface: Insights via computer simulations
    • DOI 10.1021/jp0510185
    • AA Polyansky PE Volynsky DE Nolde AS Arseniev RG Efremov 2005 Role of lipid charge in organization of water/lipid bilayer interface: Insights via computer simulations J Phys Chem B 109 15052 15059 10.1021/jp0510185 (Pubitemid 41173730)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.31 , pp. 15052-15059
    • Polyansky, A.A.1    Volynsky, P.E.2    Nolde, D.E.3    Arseniev, A.S.4    Efremov, R.G.5
  • 87
    • 33847273166 scopus 로고    scopus 로고
    • Direct demonstration of the flexibility of the glycosylated proline-threonine linker in the Cellulomonas fimi xylanase Cex through NMR spectroscopic analysis
    • DOI 10.1074/jbc.M609670200
    • DKY Poon SG Withers LP McIntosh 2007 Direct demonstration of the flexibility of the glycosylated proline-threonine linker in the Cellulomonas fimi xylanase Cex through NMR spectroscopic analysis J Biol Chem 282 2091 2100 10.1074/jbc.M609670200 (Pubitemid 47076696)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 2091-2100
    • Poon, D.K.Y.1    Withers, S.G.2    McIntosh, L.P.3
  • 88
    • 0034480326 scopus 로고    scopus 로고
    • NMR structures of biomolecules using field oriented media and residual dipolar couplings
    • DOI 10.1017/S0033583500003656
    • JH Prestegard HM Al-Hashimi JR Tolman 2000 NMR structures of biomolecules using field oriented media and residual dipolar couplings Q Rev Biophys 33 371 424 10.1017/S0033583500003656 (Pubitemid 32151707)
    • (2000) Quarterly Reviews of Biophysics , vol.33 , Issue.4 , pp. 371-424
    • Prestegard, J.H.1    Al-Hashimi, H.M.2    Tolman, J.R.3
  • 90
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • 10.1021/ja001068h
    • M Rückert G Otting 2000 Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments J Am Chem Soc 122 7793 7797 10.1021/ja001068h
    • (2000) J Am Chem Soc , vol.122 , pp. 7793-7797
    • Rückert, M.1    Otting, G.2
  • 91
    • 33846688095 scopus 로고    scopus 로고
    • Proline cis-trans Isomerization Controls Autoinhibition of a Signaling Protein
    • DOI 10.1016/j.molcel.2007.01.004, PII S1097276507000081
    • P Sarkar C Reichman T Saleh RB Birge CG Kalodimos 2007 Proline cis-trans isomerization controls autoinhibition of a signaling protein Mol Cell 25 413 426 10.1016/j.molcel.2007.01.004 (Pubitemid 46199288)
    • (2007) Molecular Cell , vol.25 , Issue.3 , pp. 413-426
    • Sarkar, P.1    Reichman, C.2    Saleh, T.3    Birge, R.B.4    Kalodimos, C.G.5
  • 93
    • 0034501042 scopus 로고    scopus 로고
    • Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes
    • DOI 10.1023/A:1026703605147
    • HJ Sass G Musco SJ Stahl PT Wingfield S Grzesiek 2000 Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes J Biomol NMR 18 303 309 10.1023/A:1026703605147 (Pubitemid 32065084)
    • (2000) Journal of Biomolecular NMR , vol.18 , Issue.4 , pp. 303-309
    • Sass, H.-J.1    Musco, G.2    J. Stahl, S.3    T. Wingfield, P.4    Grzesiek, S.5
  • 94
    • 33751157953 scopus 로고
    • Effect of ionic surfactants on nonionic bilayers: Bending elasticity of weakly charged membranes
    • 10.1021/j100065a055
    • R Schomacker R Strey 1994 Effect of ionic surfactants on nonionic bilayers: bending elasticity of weakly charged membranes J Phys Chem 98 3908 3912 10.1021/j100065a055
    • (1994) J Phys Chem , vol.98 , pp. 3908-3912
    • Schomacker, R.1    Strey, R.2
  • 95
    • 0035742323 scopus 로고    scopus 로고
    • Internal coordinates for molecular dynamics and minimization in structure determination and refinement
    • 2001JMagR.152.288S 10.1006/jmre.2001.2413
    • CD Schwieters GM Clore 2001 Internal coordinates for molecular dynamics and minimization in structure determination and refinement J Magn Reson 152 288 302 2001JMagR.152..288S 10.1006/jmre.2001.2413
    • (2001) J Magn Reson , vol.152 , pp. 288-302
    • Schwieters, C.D.1    Clore, G.M.2
  • 96
    • 0013293280 scopus 로고    scopus 로고
    • The Xplor-NIH NMR molecular structure determination package
    • 2003JMagR.160.65S 10.1016/S1090-7807(02)00014-9
    • CD Schwieters JJ Kuszewski N Tjandra GM Clore 2003 The Xplor-NIH NMR molecular structure determination package J Magn Reson 160 65 73 2003JMagR.160...65S 10.1016/S1090-7807(02)00014-9
    • (2003) J Magn Reson , vol.160 , pp. 65-73
    • Schwieters, C.D.1    Kuszewski, J.J.2    Tjandra, N.3    Clore, G.M.4
  • 97
    • 0024357911 scopus 로고
    • Formation of unique structure in polypeptide chains: Theoretical investigation with the aid of a replica approach
    • DOI 10.1016/0301-4622(89)80058-4
    • EI Shakhnovich AM Gutin 1989 Formation of unique structure in polypeptide chains. Theoretical investigation with the aid of a replica approach Biophys Chem 34 187 199 10.1016/0301-4622(89)80058-4 (Pubitemid 20007771)
    • (1989) Biophysical Chemistry , vol.34 , Issue.3 , pp. 187-199
    • Shakhnovich, E.I.1    Gutin, A.M.2
  • 98
    • 25844509280 scopus 로고    scopus 로고
    • Estimating the accuracy of protein structures using residual dipolar couplings
    • DOI 10.1007/s10858-005-2601-7
    • K Simon J Xu C Kim NR Skrynnikov 2005 Estimating the accuracy of protein structures using residual dipolar couplings J Biomol NMR 33 83 93 10.1007/s10858-005-2601-7 (Pubitemid 41662431)
    • (2005) Journal of Biomolecular NMR , vol.33 , Issue.2 , pp. 83-93
    • Simon, K.1    Xu, J.2    Kim, C.3    Skrynnikov, N.R.4
  • 99
    • 0034602921 scopus 로고    scopus 로고
    • Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin
    • 10.1006/jmbi.1999.3430
    • NR Skrynnikov NK Goto DW Yang WY Choy JR Tolman GA Mueller LE Kay 2000 Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrin J Mol Biol 295 1265 1273 10.1006/jmbi.1999.3430
    • (2000) J Mol Biol , vol.295 , pp. 1265-1273
    • Skrynnikov, N.R.1    Goto, N.K.2    Yang, D.W.3    Choy, W.Y.4    Tolman, J.R.5    Mueller, G.A.6    Kay, L.E.7
  • 100
    • 0029076557 scopus 로고
    • Calcium-induced dimerization of troponin C: Mode of interaction and use of trifluoroethanol as a denaturant of quaternary structure
    • 10.1021/bi00022a009
    • CM Slupsky CM Kay FC Reinach LB Smillie BD Sykes 1995 Calcium-induced dimerization of troponin C: mode of interaction and use of trifluoroethanol as a denaturant of quaternary structure Biochemistry 34 7365 7375 10.1021/bi00022a009
    • (1995) Biochemistry , vol.34 , pp. 7365-7375
    • Slupsky, C.M.1    Kay, C.M.2    Reinach, F.C.3    Smillie, L.B.4    Sykes, B.D.5
  • 101
    • 33846928691 scopus 로고    scopus 로고
    • Quantitative dynamics and binding studies of the 20S proteasome by NMR
    • DOI 10.1038/nature05512, PII NATURE05512
    • R Sprangers LE Kay 2007 Quantitative dynamics and binding studies of the 20S proteasome by NMR Nature 445 618 622 10.1038/nature05512 (Pubitemid 46232877)
    • (2007) Nature , vol.445 , Issue.7128 , pp. 618-622
    • Sprangers, R.1    Kay, L.E.2
  • 103
    • 0041308067 scopus 로고    scopus 로고
    • Disjoining pressure in thin liquid foam and emulsion films-new concepts and perspectives
    • 2003JPCM.15.1197S 10.1088/0953-8984/15/27/201
    • C Stubenrauch R von Klitzing 2003 Disjoining pressure in thin liquid foam and emulsion films-new concepts and perspectives J Phys Condens Matt 15 R1197 R1232 2003JPCM...15.1197S 10.1088/0953-8984/15/27/201
    • (2003) J Phys Condens Matt , vol.15
    • Stubenrauch, C.1    Von Klitzing, R.2
  • 104
    • 49649105539 scopus 로고    scopus 로고
    • Impact of phosphorylation on structure and thermodynamics of the interaction between the N-terminal domain of enzyme i and the histidine phosphocarrier protein of the bacterial phosphotransferase system
    • 10.1074/jbc.M802211200
    • JY Suh ML Cai GM Clore 2008 Impact of phosphorylation on structure and thermodynamics of the interaction between the N-terminal domain of enzyme I and the histidine phosphocarrier protein of the bacterial phosphotransferase system J Biol Chem 283 18980 18989 10.1074/jbc.M802211200
    • (2008) J Biol Chem , vol.283 , pp. 18980-18989
    • Suh, J.Y.1    Cai, M.L.2    Clore, G.M.3
  • 105
    • 0034702621 scopus 로고    scopus 로고
    • Dipole-induced ordering in nematic liquid crystals. II. The elusive holy grail
    • 2000JChPh.113.3452S 10.1063/1.1287336
    • RT Syvitski EE Burnell 2000 Dipole-induced ordering in nematic liquid crystals. II. The elusive holy grail J Chem Phys 113 3452 3465 2000JChPh.113.3452S 10.1063/1.1287336
    • (2000) J Chem Phys , vol.113 , pp. 3452-3465
    • Syvitski, R.T.1    Burnell, E.E.2
  • 106
  • 107
    • 0000095347 scopus 로고
    • Electrostatic interactions in liquid crystals: Ordering of rigid solutes in nematic solvents
    • 1994MolPh.83.847T 10.1080/00268979400101621
    • AF Terzis DJ Photinos 1994 Electrostatic interactions in liquid crystals: ordering of rigid solutes in nematic solvents Mol Phys 83 847 865 1994MolPh..83..847T 10.1080/00268979400101621
    • (1994) Mol Phys , vol.83 , pp. 847-865
    • Terzis, A.F.1    Photinos, D.J.2
  • 108
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • DOI 10.1126/science.278.5340.1111
    • N Tjandra A Bax 1997 Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium Science 278 1111 1114 1997Sci...278.1111T 10.1126/science.278.5340.1111 (Pubitemid 27517889)
    • (1997) Science , vol.278 , Issue.5340 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 109
    • 0037157124 scopus 로고    scopus 로고
    • a values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy
    • DOI 10.1021/ja020066p
    • a values of glutamate and aspartate residues in an unfolded protein by multinuclear NMR spectroscopy J Am Chem Soc 124 5714 5717 10.1021/ja020066p (Pubitemid 34533509)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.20 , pp. 5714-5717
    • Tollinger, M.1    Forman-Kay, J.D.2    Kay, L.E.3
  • 112
    • 0036652846 scopus 로고    scopus 로고
    • SH3-SH2 Domain Orientation in Src Kinases: NMR Studies of Fyn
    • DOI 10.1016/S0969-2126(02)00781-5, PII S0969212602007815
    • TS Ulmer JM Werner ID Campbell 2002 SH3-SH2 domain orientation in Src kinases: NMR studies of Fyn Structure 10 901 911 10.1016/S0969-2126(02)00781-5 (Pubitemid 34786736)
    • (2002) Structure , vol.10 , Issue.7 , pp. 901-911
    • Ulmer, T.S.1    Werner, J.M.2    Campbell, I.D.3
  • 113
    • 0042367594 scopus 로고    scopus 로고
    • Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy
    • DOI 10.1021/ja0350684
    • TS Ulmer BE Ramirez F Delaglio A Bax 2003 Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy J Am Chem Soc 125 9179 9191 10.1021/ja0350684 (Pubitemid 36903834)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.30 , pp. 9179-9191
    • Ulmer, T.S.1    Ramirez, B.E.2    Delaglio, F.3    Bax, A.4
  • 114
    • 1642363964 scopus 로고    scopus 로고
    • REDCAT: A residual dipolar coupling analysis tool
    • 2004JMagR.167.228V 10.1016/j.jmr.2003.12.012
    • H Valafar JH Prestegard 2004 REDCAT: a residual dipolar coupling analysis tool J Magn Reson 167 228 241 2004JMagR.167..228V 10.1016/j.jmr.2003.12.012
    • (2004) J Magn Reson , vol.167 , pp. 228-241
    • Valafar, H.1    Prestegard, J.H.2
  • 115
    • 33645524559 scopus 로고    scopus 로고
    • Morphology of magnetically aligning DMPC/DHPC aggregates-perforated sheets, not disks
    • 10.1021/la052988m
    • L van Dam G Karlsson K Edwards 2006 Morphology of magnetically aligning DMPC/DHPC aggregates-perforated sheets, not disks Langmuir 22 3280 3285 10.1021/la052988m
    • (2006) Langmuir , vol.22 , pp. 3280-3285
    • Van Dam, L.1    Karlsson, G.2    Edwards, K.3
  • 117
    • 0034495135 scopus 로고    scopus 로고
    • Thermodynamic and structural characterization of Asn and Ala residues in the disallowed II′ region of the Ramachandran plot
    • MC Vega JC Martínez L Serrano 2000 Thermodynamic and structural characterization of Asn and Ala residues in the disallowed II' region of the Ramachandran plot Protein Sci 9 2322 2328 10.1110/ps.9.12.2322 (Pubitemid 32105714)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2322-2328
    • Vega, M.C.1    Martinez, J.C.2    Serrano, L.3
  • 118
    • 0001209204 scopus 로고    scopus 로고
    • Weakly charged lamellar bilayer system: Interplay between thermal undulations and electrostatic repulsion
    • H von Berlepsch R de Vries 2000 Weakly charged lamellar bilayer system: interplay between thermal undulations and electrostatic repulsion Eur Phys J E1 141 152
    • (2000) Eur Phys J , vol.1 , pp. 141-152
    • Von Berlepsch, H.1    De Vries, R.2
  • 119
    • 78049339537 scopus 로고    scopus 로고
    • NMR studies on domain diffusion and alignment in modular GB1 repeats
    • 10.1016/j.bpj.2010.08.036
    • JD Walsh K Meier R Ishima AM Gronenborn 2010 NMR studies on domain diffusion and alignment in modular GB1 repeats Biophys J 99 2636 2646 10.1016/j.bpj.2010.08.036
    • (2010) Biophys J , vol.99 , pp. 2636-2646
    • Walsh, J.D.1    Meier, K.2    Ishima, R.3    Gronenborn, A.M.4
  • 120
    • 62849105308 scopus 로고    scopus 로고
    • Creating conformational entropy by increasing interdomain mobility in ligand binding regulation: A revisit to N-terminal tandem PDZ domains of PSD-95
    • 10.1021/ja8076022
    • W Wang J Weng X Zhang M Liu M Zhang 2009 Creating conformational entropy by increasing interdomain mobility in ligand binding regulation: a revisit to N-terminal tandem PDZ domains of PSD-95 J Am Chem Soc 131 787 796 10.1021/ja8076022
    • (2009) J Am Chem Soc , vol.131 , pp. 787-796
    • Wang, W.1    Weng, J.2    Zhang, X.3    Liu, M.4    Zhang, M.5
  • 121
    • 2342537095 scopus 로고    scopus 로고
    • Molecular-dynamics simulation of the effect of ions on a liquid-liquid interface for a partially miscible mixture
    • 2004JChPh.120.7681W 10.1063/1.1669374
    • KE Wardle E Carlson D Henderson RL Rowley 2004 Molecular-dynamics simulation of the effect of ions on a liquid-liquid interface for a partially miscible mixture J Chem Phys 120 7681 7688 2004JChPh.120.7681W 10.1063/1.1669374
    • (2004) J Chem Phys , vol.120 , pp. 7681-7688
    • Wardle, K.E.1    Carlson, E.2    Henderson, D.3    Rowley, R.L.4
  • 122
    • 33746888255 scopus 로고    scopus 로고
    • Adaptor molecule Crk is required for sustained phosphorylation of Grb2-associated binder 1 and hepatocyte growth factor-induced cell motility of human synovial sarcoma cell lines
    • DOI 10.1158/1541-7786.MCR-05-0141
    • T Watanabe M Tsuda Y Makino S Ichihara H Sawa A Minami N Mochizuki K Nagashima S Tanaka 2006 Adaptor molecule Crk is required for sustained phosphorylation of Grb2-associated binder 1 and hepatocyte growth factor-induced cell motility of human synovial sarcoma cell lines Mol Cancer Res 4 499 510 10.1158/1541-7786.MCR-05-0141 (Pubitemid 44197045)
    • (2006) Molecular Cancer Research , vol.4 , Issue.7 , pp. 499-510
    • Watanabe, T.1    Tsuda, M.2    Makino, Y.3    Ichihara, S.4    Sawa, H.5    Minami, A.6    Mochizuki, N.7    Nagashima, K.8    Tanaka, S.9
  • 123
    • 67650482706 scopus 로고    scopus 로고
    • Influence of the coupling of interdomain and overall motions on NMR relaxation
    • 2009PNAS.10611016W 10.1073/pnas.0809994106
    • V Wong DA Case A Szabo 2009 Influence of the coupling of interdomain and overall motions on NMR relaxation Proc Natl Acad Sci USA 106 11016 11021 2009PNAS..10611016W 10.1073/pnas.0809994106
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11016-11021
    • Wong, V.1    Case, D.A.2    Szabo, A.3
  • 124
    • 33745607601 scopus 로고    scopus 로고
    • Prediction of molecular alignment of nucleic acids in aligned media
    • DOI 10.1007/s10858-006-9004-2
    • B Wu M Petersen F Girard M Tessari SS Wijmenga 2006 Prediction of molecular alignment of nucleic acids in aligned media J Biomol NMR 35 103 115 10.1007/s10858-006-9004-2 (Pubitemid 43986213)
    • (2006) Journal of Biomolecular NMR , vol.35 , Issue.2 , pp. 103-115
    • Wu, B.1    Petersen, M.2    Girard, F.3    Tessari, M.4    Wijmenga, S.S.5
  • 125
    • 0000077447 scopus 로고    scopus 로고
    • A sensitivity-enhanced method for measuring heteronuclear long-rangé coupling constants from the displacement of signals in two 1D subspectra
    • DW Yang K Nagayama 1996 A sensitivity-enhanced method for measuring heteronuclear long-range coupling constants from the displacement of signals in two 1D subspectra J Magn Reson Ser A 118 117 121 10.1006/jmra.1996.0017 (Pubitemid 126751682)
    • (1996) Journal of Magnetic Resonance - Series A , vol.118 , Issue.1 , pp. 117-121
    • Yang, D.1    Nagayama, K.2
  • 126
    • 13944258422 scopus 로고    scopus 로고
    • Physisorption of hydroxide ions from aqueous solution to a hydrophobic surface
    • DOI 10.1021/ja044426f
    • R Zangi JBFN Engberts 2005 Physisorption of hydroxide ions from aqueous solution to a hydrophobic surface J Am Chem Soc 127 2272 2276 10.1021/ja044426f (Pubitemid 40270532)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.7 , pp. 2272-2276
    • Zangi, R.1    Engberts, J.B.F.N.2
  • 127
    • 3142677815 scopus 로고    scopus 로고
    • The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains
    • DOI 10.1073/pnas.0401313101
    • YB Zhang ERP Zuiderweg 2004 The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains Proc Natl Acad Sci USA 101 10272 10277 2004PNAS..10110272Z 10.1073/pnas.0401313101 (Pubitemid 38924915)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.28 , pp. 10272-10277
    • Zhang, Y.1    Zuiderweg, E.R.P.2
  • 128
    • 50149105176 scopus 로고    scopus 로고
    • Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling
    • 2008PNAS.10511760Z 10.1073/pnas.0708583105
    • YJ Zhang H Oh RA Burton JW Burgner RL Geahlen CB Post 2008 Tyr130 phosphorylation triggers Syk release from antigen receptor by long-distance conformational uncoupling Proc Natl Acad Sci USA 105 11760 11765 2008PNAS..10511760Z 10.1073/pnas.0708583105
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 11760-11765
    • Zhang, Y.J.1    Oh, H.2    Burton, R.A.3    Burgner, J.W.4    Geahlen, R.L.5    Post, C.B.6
  • 129
    • 5444268689 scopus 로고    scopus 로고
    • Molecular simulation study of water interactions with oligo (ethylene glycol)-terminated alkanethiol self-assembled monolayers
    • 10.1021/la036345n
    • J Zheng LY Li SF Chen SY Jiang 2004 Molecular simulation study of water interactions with oligo (ethylene glycol)-terminated alkanethiol self-assembled monolayers Langmuir 20 8931 8938 10.1021/la036345n
    • (2004) Langmuir , vol.20 , pp. 8931-8938
    • Zheng, J.1    Li, L.Y.2    Chen, S.F.3    Jiang, S.Y.4
  • 130
    • 23244447443 scopus 로고    scopus 로고
    • Strong repulsive forces between protein and oligo (ethylene glycol) self-assembled monolayers: A molecular simulation study
    • DOI 10.1529/biophysj.105.059428
    • J Zheng LY Li HK Tsao YJ Sheng SF Chen SY Jiang 2005 Strong repulsive forces between protein and oligo (ethylene glycol) self-assembled monolayers: A molecular simulation study Biophys J 89 158 166 10.1529/biophysj.105.059428 (Pubitemid 41098272)
    • (2005) Biophysical Journal , vol.89 , Issue.1 , pp. 158-166
    • Zheng, J.1    Li, L.2    Tsao, H.-K.3    Sheng, Y.-J.4    Chen, S.5    Jiang, S.6
  • 131
    • 29944441649 scopus 로고    scopus 로고
    • Prediction of charge-induced molecular alignment: Residual dipolar couplings at pH 3 and alignment in surfactant liquid crystalline phases
    • DOI 10.1007/s00249-005-0018-6
    • M Zweckstetter 2006 Prediction of charge-induced molecular alignment: residual dipolar couplings at pH 3 and alignment in surfactant liquid crystalline phases Eur Biophys J Biophys Lett 35 170 180 10.1007/s00249-005- 0018-6 (Pubitemid 43042776)
    • (2006) European Biophysics Journal , vol.35 , Issue.2 , pp. 170-180
    • Zweckstetter, M.1
  • 132
    • 42149130389 scopus 로고    scopus 로고
    • NMR: Prediction of molecular alignment from structure using the PALES software
    • DOI 10.1038/nprot.2008.36, PII NPROT.2008.36
    • M Zweckstetter 2008 NMR: prediction of molecular alignment from structure using the PALES software Nat Protoc 3 679 690 10.1038/nprot.2008.36 (Pubitemid 351522648)
    • (2008) Nature Protocols , vol.3 , Issue.4 , pp. 679-690
    • Zweckstetter, M.1
  • 133
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR [11]
    • DOI 10.1021/ja0000908
    • M Zweckstetter A Bax 2000 Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR J Am Chem Soc 122 3791 3792 10.1021/ja0000908 (Pubitemid 30233459)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.15 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 134
    • 2942653357 scopus 로고    scopus 로고
    • Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases
    • DOI 10.1529/biophysj.103.035790
    • M Zweckstetter G Hummer A Bax 2004 Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases Biophys J 86 3444 3460 10.1529/biophysj.103.035790 (Pubitemid 38780229)
    • (2004) Biophysical Journal , vol.86 , Issue.6 , pp. 3444-3460
    • Zweckstetter, M.1    Hummer, G.2    Bax, A.3


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