메뉴 건너뛰기




Volumn 47, Issue 10, 2014, Pages 3118-3126

Insights into domain-domain motions in proteins and RNA from solution NMR

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; RNA;

EID: 84908093659     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar5002318     Document Type: Article
Times cited : (34)

References (62)
  • 2
  • 4
    • 0033784534 scopus 로고    scopus 로고
    • Induced Fit in RNA-Protein Recognition
    • Williamson, J. R. Induced Fit in RNA-Protein Recognition Nat. Struct. Biol. 2000, 7, 834-837
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 834-837
    • Williamson, J.R.1
  • 5
    • 84857080591 scopus 로고    scopus 로고
    • Functional Complexity and Regulation Through RNA Dynamics
    • Dethoff, E. A.; Chugh, J.; Mustoe, A. M.; Al Hashimi, H. M. Functional Complexity and Regulation Through RNA Dynamics Nature 2012, 482, 322-330
    • (2012) Nature , vol.482 , pp. 322-330
    • Dethoff, E.A.1    Chugh, J.2    Mustoe, A.M.3    Al Hashimi, H.M.4
  • 6
    • 33846230547 scopus 로고    scopus 로고
    • "four-Dimensional" Protein Structures: Examples from Metalloproteins
    • Fragai, M.; Luchinat, C.; Parigi, G. "Four-Dimensional" Protein Structures: Examples From Metalloproteins Acc. Chem. Res. 2006, 39, 909-917
    • (2006) Acc. Chem. Res. , vol.39 , pp. 909-917
    • Fragai, M.1    Luchinat, C.2    Parigi, G.3
  • 8
    • 14844353335 scopus 로고    scopus 로고
    • Recent Progress in the Study of Biomolecular Structure and Dynamics in Solution from Residual Dipolar Couplings
    • Blackledge, M. Recent Progress in the Study of Biomolecular Structure and Dynamics in Solution From Residual Dipolar Couplings Prog. NMR Spectrosc. 2005, 46, 23-61
    • (2005) Prog. NMR Spectrosc. , vol.46 , pp. 23-61
    • Blackledge, M.1
  • 11
    • 37549017736 scopus 로고    scopus 로고
    • Visualizing Spatially Correlated Dynamics That Directs RNA Conformational Transitions
    • Zhang, Q.; Stelzer, A. C.; Fisher, C. K.; Al-Hashimi, H. M. Visualizing Spatially Correlated Dynamics That Directs RNA Conformational Transitions Nature 2007, 450, 1263-1267
    • (2007) Nature , vol.450 , pp. 1263-1267
    • Zhang, Q.1    Stelzer, A.C.2    Fisher, C.K.3    Al-Hashimi, H.M.4
  • 12
    • 71749087100 scopus 로고    scopus 로고
    • Quantitative Description of Backbone Conformational Sampling of Unfolded Proteins at Amino Acid Resolution from NMR Residual Dipolar Couplings
    • Nodet, L.; Salmon, L.; Ozenne, V.; Meier, S.; Jensen, M. R.; Blackledge, M. Quantitative Description of Backbone Conformational Sampling of Unfolded Proteins at Amino Acid Resolution From NMR Residual Dipolar Couplings J. Am. Chem. Soc. 2009, 131, 17908-17918
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17908-17918
    • Nodet, L.1    Salmon, L.2    Ozenne, V.3    Meier, S.4    Jensen, M.R.5    Blackledge, M.6
  • 14
    • 34848845491 scopus 로고    scopus 로고
    • Deciphering Protein Dynamics from NMR Data Using Explicit Structure Sampling and Selection
    • Chen, Y.; Campbell, S. L.; Dokholyan, N. V. Deciphering Protein Dynamics From NMR Data Using Explicit Structure Sampling and Selection Biophys. J. 2007, 93, 2300-2306
    • (2007) Biophys. J. , vol.93 , pp. 2300-2306
    • Chen, Y.1    Campbell, S.L.2    Dokholyan, N.V.3
  • 15
    • 84897523651 scopus 로고    scopus 로고
    • Advances in the Determination of Nucleic Acid Conformational Ensembles
    • Salmon, L.; Yang, S.; Al Hashimi, H. M. Advances in the Determination of Nucleic Acid Conformational Ensembles Annu. Rev. Phys. Chem. 2014, 65, 293-316
    • (2014) Annu. Rev. Phys. Chem. , vol.65 , pp. 293-316
    • Salmon, L.1    Yang, S.2    Al Hashimi, H.M.3
  • 16
    • 33646931175 scopus 로고    scopus 로고
    • NMR Residual Dipolar Couplings As Probes of Biomolecular Dynamics
    • Tolman, J. R.; Ruan, K. NMR Residual Dipolar Couplings As Probes of Biomolecular Dynamics Chem. Rev. 2006, 106, 1720-1736
    • (2006) Chem. Rev. , vol.106 , pp. 1720-1736
    • Tolman, J.R.1    Ruan, K.2
  • 17
    • 0030722243 scopus 로고    scopus 로고
    • Direct Measurement of Distances and Angles in Biomolecules by NMR in a Diluite Liquid Crystalline Medium
    • Tjandra, N.; Bax, A. Direct Measurement of Distances and Angles in Biomolecules by NMR in a Diluite Liquid Crystalline Medium Science 1997, 278, 1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 18
    • 0031760503 scopus 로고    scopus 로고
    • Tunable Alignment of Macromolecules by Filamentous Phage Yields Dipolar Coupling Interactions
    • Hansen, M. R.; Mueller, L.; Pardi, A. Tunable Alignment of Macromolecules by Filamentous Phage Yields Dipolar Coupling Interactions Nat. Struct. Biol. 1998, 5, 1065-1074
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1065-1074
    • Hansen, M.R.1    Mueller, L.2    Pardi, A.3
  • 19
    • 0029050883 scopus 로고
    • Nuclear Magnetic Dipole Interactions in Field-Oriented Proteins: Information for Structure Determination in Solution
    • Tolman, J. R.; Flanagan, J. M.; Kennedy, M. A.; Prestegard, J. H. Nuclear Magnetic Dipole Interactions in Field-Oriented Proteins: Information for Structure Determination in Solution Proc. Natl. Acad. Sci. U.S.A. 1995, 92, 9279-9283
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 9279-9283
    • Tolman, J.R.1    Flanagan, J.M.2    Kennedy, M.A.3    Prestegard, J.H.4
  • 20
    • 0042355704 scopus 로고    scopus 로고
    • Probing Motions between Equivalent RNA Domains Using Magnetic Field Induced Residual Dipolar Couplings: Accounting for Correlations between Motions and Alignment
    • Zhang, Q.; Throolin, R.; Pitt, S. W.; Serganov, A.; Al Hashimi, H. M. Probing Motions Between Equivalent RNA Domains Using Magnetic Field Induced Residual Dipolar Couplings: Accounting for Correlations Between Motions and Alignment J. Am. Chem. Soc. 2003, 125, 10530-10531
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10530-10531
    • Zhang, Q.1    Throolin, R.2    Pitt, S.W.3    Serganov, A.4    Al Hashimi, H.M.5
  • 21
    • 55549133637 scopus 로고    scopus 로고
    • Design, Synthesis, and Evaluation of a Lanthanide Chelating Protein Probe: CLaNP-5 Yields Predictable Paramagnetic Effects Independent of Environment
    • Keizers, P. H. J.; Saragliadis, A.; Hiruma, Y.; Overhand, M.; Ubbink, M. Design, Synthesis, and Evaluation of a Lanthanide Chelating Protein Probe: CLaNP-5 Yields Predictable Paramagnetic Effects Independent of Environment J. Am. Chem. Soc. 2008, 130, 14802-14812
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 14802-14812
    • Keizers, P.H.J.1    Saragliadis, A.2    Hiruma, Y.3    Overhand, M.4    Ubbink, M.5
  • 24
    • 0034293196 scopus 로고    scopus 로고
    • Lanthanide Ions Bind Specifically to an Added "eF-Hand" and Orient a Membrane Protein in Micelles for Solution NMR Spectroscopy
    • Ma, C.; Opella, S. J. Lanthanide Ions Bind Specifically to an Added "EF-Hand" and Orient a Membrane Protein in Micelles for Solution NMR Spectroscopy J. Magn. Reson. 2000, 146, 381-384
    • (2000) J. Magn. Reson. , vol.146 , pp. 381-384
    • Ma, C.1    Opella, S.J.2
  • 25
    • 34147204158 scopus 로고    scopus 로고
    • NMR Structure Determination of Protein-Ligand Complexes by Lanthanide Labeling
    • Pintacuda, G.; John, M.; Su, X. C.; Otting, G. NMR Structure Determination of Protein-Ligand Complexes by Lanthanide Labeling Acc. Chem. Res. 2007, 40, 206-212
    • (2007) Acc. Chem. Res. , vol.40 , pp. 206-212
    • Pintacuda, G.1    John, M.2    Su, X.C.3    Otting, G.4
  • 26
    • 0242299265 scopus 로고    scopus 로고
    • Protein Alignment by a Coexpressed Lanthanide-Binding Tag for the Measurement of Residual Dipolar Couplings
    • Wöhnert, J.; Franz, K. J.; Nitz, M.; Imperiali, B.; Schwalbe, H. Protein Alignment by a Coexpressed Lanthanide-Binding Tag for the Measurement of Residual Dipolar Couplings J. Am. Chem. Soc. 2003, 125, 13338-13339
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13338-13339
    • Wöhnert, J.1    Franz, K.J.2    Nitz, M.3    Imperiali, B.4    Schwalbe, H.5
  • 27
    • 0032177976 scopus 로고    scopus 로고
    • NMR Structure Determination of Proteins and Protein Complexes Larger Than 20 KDa
    • Clore, G. M.; Gronenborn, A. M. NMR Structure Determination of Proteins and Protein Complexes Larger Than 20 KDa Curr. Opin. Chem. Biol. 1998, 2, 564-570
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 564-570
    • Clore, G.M.1    Gronenborn, A.M.2
  • 28
    • 80755127361 scopus 로고    scopus 로고
    • Domain Cooperativity in Multidomain Proteins: What Can We Learn from Molecular Alignment in Anisotropic Media?
    • Yuwen, T.; Post, C. B.; Skrynnikov, N. R. Domain Cooperativity in Multidomain Proteins: What Can We Learn From Molecular Alignment in Anisotropic Media? J. Biomol. NMR 2011, 51, 131-150
    • (2011) J. Biomol. NMR , vol.51 , pp. 131-150
    • Yuwen, T.1    Post, C.B.2    Skrynnikov, N.R.3
  • 29
    • 38349001213 scopus 로고    scopus 로고
    • Comparison of Alignment Tensors Generated for Native TRNA(Val) Using Magnetic Fields and Liquid Crystalline Media
    • Latham, M. P.; Hanson, P.; Brown, D. J.; Pardi, A. Comparison of Alignment Tensors Generated for Native TRNA(Val) Using Magnetic Fields and Liquid Crystalline Media J. Biomol. NMR 2008, 40, 83-94
    • (2008) J. Biomol. NMR , vol.40 , pp. 83-94
    • Latham, M.P.1    Hanson, P.2    Brown, D.J.3    Pardi, A.4
  • 30
    • 84882890430 scopus 로고    scopus 로고
    • Conformational Freedom of Metalloproteins Revealed by Paramagnetism-Assisted NMR
    • Fragai, M.; Luchinat, C.; Parigi, G.; Ravera, E. Conformational Freedom of Metalloproteins Revealed by Paramagnetism-Assisted NMR Coord. Chem. Rev. 2013, 257, 2652-2667
    • (2013) Coord. Chem. Rev. , vol.257 , pp. 2652-2667
    • Fragai, M.1    Luchinat, C.2    Parigi, G.3    Ravera, E.4
  • 31
    • 79952106662 scopus 로고    scopus 로고
    • Moving the Frontiers in Solution Solid State BioNMR. A Celebration of Harry Gray"s 75th Birthday
    • Bertini, I.; Luchinat, C.; Parigi, G. Moving the Frontiers in Solution Solid State BioNMR. A Celebration of Harry Gray"s 75th Birthday Coord. Chem. Rev. 2011, 255, 649-663
    • (2011) Coord. Chem. Rev. , vol.255 , pp. 649-663
    • Bertini, I.1    Luchinat, C.2    Parigi, G.3
  • 32
    • 0032539192 scopus 로고    scopus 로고
    • 5 at High Magnetic Fields: Magnetic Susceptibility Anisotropy Contributions and Consequences for Protein Solution Structure Determination
    • 5 at High Magnetic Fields: Magnetic Susceptibility Anisotropy Contributions and Consequences for Protein Solution Structure Determination J. Am. Chem. Soc. 1998, 120, 12903-12909
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 12903-12909
    • Banci, L.1    Bertini, I.2    Huber, J.G.3    Luchinat, C.4    Rosato, A.5
  • 33
    • 0034685602 scopus 로고    scopus 로고
    • De Novo Determination of Protein Structure by NMR Using Orientational and Long-Range Order Restraints
    • Hus, J. C.; Marion, D.; Blackledge, M. De Novo Determination of Protein Structure by NMR Using Orientational and Long-Range Order Restraints J. Mol. Biol. 2000, 298, 927-936
    • (2000) J. Mol. Biol. , vol.298 , pp. 927-936
    • Hus, J.C.1    Marion, D.2    Blackledge, M.3
  • 35
    • 67849117178 scopus 로고    scopus 로고
    • Accurate Solution Structures of Proteins from X-Ray Data and Minimal Set of NMR Data: Calmodulin Peptide Complexes As Examples
    • Bertini, I.; Kursula, P.; Luchinat, C.; Parigi, G.; Vahokoski, J.; Willmans, M.; Yuan, J. Accurate Solution Structures of Proteins From X-Ray Data and Minimal Set of NMR Data: Calmodulin Peptide Complexes As Examples J. Am. Chem. Soc. 2009, 131, 5134-5144
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5134-5144
    • Bertini, I.1    Kursula, P.2    Luchinat, C.3    Parigi, G.4    Vahokoski, J.5    Willmans, M.6    Yuan, J.7
  • 36
    • 31944446215 scopus 로고    scopus 로고
    • Resolving the Motional Modes That Code for RNA Adaptation
    • Zhang, Q.; Sun, X.; Watt, E. D.; Al Hashimi, H. M. Resolving the Motional Modes That Code for RNA Adaptation Science 2006, 311, 653-656
    • (2006) Science , vol.311 , pp. 653-656
    • Zhang, Q.1    Sun, X.2    Watt, E.D.3    Al Hashimi, H.M.4
  • 37
    • 84865640552 scopus 로고    scopus 로고
    • Independent Alignment of RNA for Dynamic Studies Using Residual Dipolar Couplings
    • Bardaro, M. F., Jr.; Varani, G. Independent Alignment of RNA for Dynamic Studies Using Residual Dipolar Couplings J. Biomol. NMR 2012, 54, 69-80
    • (2012) J. Biomol. NMR , vol.54 , pp. 69-80
    • Bardaro, M.F.1    Varani, G.2
  • 38
    • 0030963093 scopus 로고    scopus 로고
    • Defining Long Range Order in NMR Structure Determination from the Dependence of Heteronuclear Relaxation Times on Rotational Diffusion Anisotropy
    • Tjandra, N.; Garrett, D. S.; Gronenborn, A. M.; Bax, A.; Clore, G. M. Defining Long Range Order in NMR Structure Determination From the Dependence of Heteronuclear Relaxation Times on Rotational Diffusion Anisotropy Nat. Struct. Biol. 1997, 4, 443-449
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 443-449
    • Tjandra, N.1    Garrett, D.S.2    Gronenborn, A.M.3    Bax, A.4    Clore, G.M.5
  • 39
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of Sterically Induced Alignment in a Dilute Liquid Crystalline Phase: Aid to Protein Structure Determination by NMR
    • Zweckstetter, M.; Bax, A. Prediction of Sterically Induced Alignment in a Dilute Liquid Crystalline Phase: Aid to Protein Structure Determination by NMR J. Am. Chem. Soc. 2000, 122, 3791-3792
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 40
    • 84876030925 scopus 로고    scopus 로고
    • A General Method for Constructing Atomic-Resolution RNA Ensembles Using NMR Residual Dipolar Couplings: The Basis for Interhelical Motions Revealed
    • Salmon, L.; Bascom, G.; Andricioaei, I.; Al Hashimi, H. M. A General Method for Constructing Atomic-Resolution RNA Ensembles Using NMR Residual Dipolar Couplings: the Basis for Interhelical Motions Revealed J. Am. Chem. Soc. 2013, 135, 5457-5466
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 5457-5466
    • Salmon, L.1    Bascom, G.2    Andricioaei, I.3    Al Hashimi, H.M.4
  • 41
    • 0033551495 scopus 로고    scopus 로고
    • Domain Orientation and Dynamics in Multidomain Proteins from Residual Dipolar Couplings
    • Fischer, M. W.; Losonczi, J. A.; Weaver, J. L.; Prestegard, J. H. Domain Orientation and Dynamics in Multidomain Proteins From Residual Dipolar Couplings Biochemistry 1999, 38, 9013-9022
    • (1999) Biochemistry , vol.38 , pp. 9013-9022
    • Fischer, M.W.1    Losonczi, J.A.2    Weaver, J.L.3    Prestegard, J.H.4
  • 42
    • 67649891135 scopus 로고    scopus 로고
    • Constructing RNA Dynamical Ensembles by Combining MD and Motionally Decoupled NMR RDCs: New Insights into RNA Dynamics and Adaptive Ligand Recognition
    • Frank, A. T.; Stelzer, A. C.; Al-Hashimi, H. M.; Andricioaei, I. Constructing RNA Dynamical Ensembles by Combining MD and Motionally Decoupled NMR RDCs: New Insights into RNA Dynamics and Adaptive Ligand Recognition Nucleic Acids Res. 2009, 37, 3670-3679
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3670-3679
    • Frank, A.T.1    Stelzer, A.C.2    Al-Hashimi, H.M.3    Andricioaei, I.4
  • 43
    • 0027384192 scopus 로고
    • Conformational Backbone Dynamics of the Cyclic Decapeptide Antamanide. Application of a New Multiconformational Search Algorithm Based on NMR Data
    • Blackledge, M. J.; Bruschweiler, R.; Griesinger, C.; Schmidt, J. M.; Xu, P.; Ernst, R. R. Conformational Backbone Dynamics of the Cyclic Decapeptide Antamanide. Application of a New Multiconformational Search Algorithm Based on NMR Data Biochemistry 1993, 32, 10960-10974
    • (1993) Biochemistry , vol.32 , pp. 10960-10974
    • Blackledge, M.J.1    Bruschweiler, R.2    Griesinger, C.3    Schmidt, J.M.4    Xu, P.5    Ernst, R.R.6
  • 44
    • 0032879507 scopus 로고    scopus 로고
    • R-Factor, Free R, and Complete Cross-Validation for Dipolar Coupling Refinement of NMR Structures
    • Clore, G. M.; Garrett, D. S. R-Factor, Free R, and Complete Cross-Validation for Dipolar Coupling Refinement of NMR Structures J. Am. Chem. Soc. 1999, 121, 9008-9012
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 9008-9012
    • Clore, G.M.1    Garrett, D.S.2
  • 45
    • 84899936219 scopus 로고    scopus 로고
    • Measuring Similarity between Dynamic Ensembles of Biomolecules
    • Yang, S.; Salmon, L.; Al Hashimi, H. M. Measuring Similarity Between Dynamic Ensembles of Biomolecules Nat. Methods 2014, 11, 552-554
    • (2014) Nat. Methods , vol.11 , pp. 552-554
    • Yang, S.1    Salmon, L.2    Al Hashimi, H.M.3
  • 48
    • 0026748968 scopus 로고
    • 15N Relaxation Using Inverse Detected Two-Dimensional NMR Spectroscopy; The Central Helix is Flexible
    • 15N Relaxation Using Inverse Detected Two-Dimensional NMR Spectroscopy; the Central Helix Is Flexible Biochemistry 1992, 31, 5269-5278
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 50
    • 84862303541 scopus 로고    scopus 로고
    • Paramagnetic Relaxation Enhancements for the Characterization of the Conformational Heterogeneity in Two-Domain Proteins
    • Bertini, I.; Luchinat, C.; Nagulapalli, M.; Parigi, G.; Ravera, E. Paramagnetic Relaxation Enhancements for the Characterization of the Conformational Heterogeneity in Two-Domain Proteins Phys. Chem. Chem. Phys. 2012, 14, 9149-9156
    • (2012) Phys. Chem. Chem. Phys. , vol.14 , pp. 9149-9156
    • Bertini, I.1    Luchinat, C.2    Nagulapalli, M.3    Parigi, G.4    Ravera, E.5
  • 52
    • 74249115345 scopus 로고    scopus 로고
    • Topology Links RNA Secondary Structure with Global Conformation, Dynamics, and Adaptation
    • Bailor, M. H.; Sun, X.; Al Hashimi, H. M. Topology Links RNA Secondary Structure With Global Conformation, Dynamics, and Adaptation Science 2010, 327, 202-206
    • (2010) Science , vol.327 , pp. 202-206
    • Bailor, M.H.1    Sun, X.2    Al Hashimi, H.M.3
  • 53
    • 73249135897 scopus 로고    scopus 로고
    • Do Conformational Biases of Simple Helical Junctions Influence RNA Folding Stability and Specificity?
    • Chu, V. B.; Lipfert, J.; Bai, Y.; Pande, V. S.; Doniach, S.; Herschlag, D. Do Conformational Biases of Simple Helical Junctions Influence RNA Folding Stability and Specificity? RNA 2009, 15, 2195-2205
    • (2009) RNA , vol.15 , pp. 2195-2205
    • Chu, V.B.1    Lipfert, J.2    Bai, Y.3    Pande, V.S.4    Doniach, S.5    Herschlag, D.6
  • 54
    • 84855902184 scopus 로고    scopus 로고
    • New Insights into the Fundamental Role of Topological Constraints As a Determinant of Two-Way Junction Conformation
    • Mustoe, A. M.; Bailor, M. H.; Teixeira, R. M.; Brooks, C. L., III; Al Hashimi, H. M. New Insights into the Fundamental Role of Topological Constraints As a Determinant of Two-Way Junction Conformation Nucleic Acids Res. 2012, 40, 892-904
    • (2012) Nucleic Acids Res. , vol.40 , pp. 892-904
    • Mustoe, A.M.1    Bailor, M.H.2    Teixeira, R.M.3    Brooks, C.4    Al Hashimi, H.M.5
  • 56
    • 84896300726 scopus 로고    scopus 로고
    • Coarse Grained Models Reveal Essential Contributions of Topological Constraints to the Conformational Free Energy of RNA Bulges
    • Mustoe, A. M.; Al Hashimi, H. M.; Brooks, C. L., III. Coarse Grained Models Reveal Essential Contributions of Topological Constraints to the Conformational Free Energy of RNA Bulges J. Phys. Chem. B 2014, 118, 2615-2627
    • (2014) J. Phys. Chem. B , vol.118 , pp. 2615-2627
    • Mustoe, A.M.1    Al Hashimi, H.M.2    Iii., L.B.C.3
  • 57
    • 0242593434 scopus 로고    scopus 로고
    • Development and Current Status of the CHARMM Force Field for Nucleic Acids
    • Mackerell, A. D., Jr.; Banavali, N.; Foloppe, N. Development and Current Status of the CHARMM Force Field for Nucleic Acids Biopolymers 2000, 56, 257-265
    • (2000) Biopolymers , vol.56 , pp. 257-265
    • Mackerell, A.D.1    Banavali, N.2    Foloppe, N.3
  • 59
    • 0033581191 scopus 로고    scopus 로고
    • Characterization of N-15 Chemical Shift Anisotropy from Orientation-Dependent Changes to N-15 Chemical Shifts in Dilute Bicelle Solutions
    • Boyd, J.; Redfield, C. Characterization of N-15 Chemical Shift Anisotropy From Orientation-Dependent Changes to N-15 Chemical Shifts in Dilute Bicelle Solutions J. Am. Chem. Soc. 1999, 121, 7441-7442
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7441-7442
    • Boyd, J.1    Redfield, C.2
  • 62
    • 0000676854 scopus 로고
    • Alignment Effects on High Resolution NMR Spectra Induced by the Magnetic Field
    • Lohman, J. A. B.; Maclean, C. Alignment Effects on High Resolution NMR Spectra Induced by the Magnetic Field Chem. Phys. 1978, 35, 269-274
    • (1978) Chem. Phys. , vol.35 , pp. 269-274
    • Lohman, J.A.B.1    Maclean, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.