On the use of residual dipolar couplings in multi-state structure calculation of two-domain proteins
Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of indiv...
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| Vydáno v: | Magnetic resonance letters Ročník 2; číslo 2; s. 61 - 68 |
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| Médium: | Journal Article |
| Jazyk: | angličtina |
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Elsevier B.V
01.05.2022
KeAi Communications Co. Ltd |
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| ISSN: | 2772-5162, 2097-0048, 2772-5162 |
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| Abstract | Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of individual bond vectors or simultaneously with this refinement. For single-domain proteins this approach works well since all bond vectors can be described within the same coordinate frame, which is given by the alignment tensor. However, novel approaches are sought after for systems where no universal alignment tensor can be used. Here, we present an approach that can be applied to two-domain proteins that enables the calculation of multiple states within each domain as well as with respect to the relative positions of the two domains.
The use of residual dipolar couplings in multi-state structure calculation with two-domain proteins is challenge. Here we present a protocol that relies on a two-step calculation using alignment tensors of both domains. [Display omitted] |
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| AbstractList | Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of individual bond vectors or simultaneously with this refinement. For single-domain proteins this approach works well since all bond vectors can be described within the same coordinate frame, which is given by the alignment tensor. However, novel approaches are sought after for systems where no universal alignment tensor can be used. Here, we present an approach that can be applied to two-domain proteins that enables the calculation of multiple states within each domain as well as with respect to the relative positions of the two domains.Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of individual bond vectors or simultaneously with this refinement. For single-domain proteins this approach works well since all bond vectors can be described within the same coordinate frame, which is given by the alignment tensor. However, novel approaches are sought after for systems where no universal alignment tensor can be used. Here, we present an approach that can be applied to two-domain proteins that enables the calculation of multiple states within each domain as well as with respect to the relative positions of the two domains. Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of individual bond vectors or simultaneously with this refinement. For single-domain proteins this approach works well since all bond vectors can be described within the same coordinate frame, which is given by the alignment tensor. However, novel approaches are sought after for systems where no universal alignment tensor can be used. Here, we present an approach that can be applied to two-domain proteins that enables the calculation of multiple states within each domain as well as with respect to the relative positions of the two domains. The use of residual dipolar couplings in multi-state structure calculation with two-domain proteins is challenge. Here we present a protocol that relies on a two-step calculation using alignment tensors of both domains. [Display omitted] Residual dipolar couplings (RDCs) are powerful nuclear magnetic resonance (NMR) probes for the structure calculation of biomacromolecules. Typically, an alignment tensor that defines the orientation of the entire molecule relative to the magnetic field is determined either before refinement of individual bond vectors or simultaneously with this refinement. For single-domain proteins this approach works well since all bond vectors can be described within the same coordinate frame, which is given by the alignment tensor. However, novel approaches are sought after for systems where no universal alignment tensor can be used. Here, we present an approach that can be applied to two-domain proteins that enables the calculation of multiple states within each domain as well as with respect to the relative positions of the two domains. |
| Author | Born, Alexandra Nichols, Parker J. Henen, Morkos A. Vögeli, Beat |
| AuthorAffiliation | 2 Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt 1 University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics, 12801 East 17 th Avenue, Aurora, CO 80045, USA |
| AuthorAffiliation_xml | – name: 1 University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics, 12801 East 17 th Avenue, Aurora, CO 80045, USA – name: 2 Faculty of Pharmacy, Mansoura University, Mansoura, 35516, Egypt |
| Author_xml | – sequence: 1 givenname: Alexandra surname: Born fullname: Born, Alexandra organization: University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics, 12801 East 17th Avenue, Aurora, CO, 80045, USA – sequence: 2 givenname: Morkos A. surname: Henen fullname: Henen, Morkos A. organization: University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics, 12801 East 17th Avenue, Aurora, CO, 80045, USA – sequence: 3 givenname: Parker J. orcidid: 0000-0003-1930-6408 surname: Nichols fullname: Nichols, Parker J. organization: University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics, 12801 East 17th Avenue, Aurora, CO, 80045, USA – sequence: 4 givenname: Beat orcidid: 0000-0003-1176-3137 surname: Vögeli fullname: Vögeli, Beat email: beat.vogeli@cuanschutz.edu organization: University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics, 12801 East 17th Avenue, Aurora, CO, 80045, USA |
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| Cites_doi | 10.1016/j.pnmrs.2004.02.001 10.1016/j.pbiomolbio.2013.05.001 10.1126/science.278.5345.1957 10.3390/molecules22071176 10.1016/j.pnmrs.2013.11.001 10.1021/jacs.1c06289 10.1038/380544a0 10.1006/jmre.1999.1754 10.1080/00268976.2012.728257 10.1021/ja0386804 10.1021/ja067667r 10.1016/bs.mie.2015.06.032 10.1126/science.278.5340.1111 10.1074/jbc.M300796200 10.1021/bi000060h 10.1002/cbic.201800237 10.1007/s00249-008-0367-z 10.1021/jz301788n 10.1023/B:JNMR.0000019499.60777.6e 10.1016/S0092-8674(00)80273-1 10.1021/ja00901a059 10.1016/j.jmb.2018.05.007 10.1002/anie.202008734 10.1073/pnas.1019382108 10.1021/ja000858o 10.1007/s10858-015-9917-8 10.1021/cr040429z 10.1074/jbc.M300721200 10.1007/s12551-015-0171-9 10.1021/ja0726613 |
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| Keywords | RDC Residual dipolar coupling Two-domain protein Multi-state structure |
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| References | Strotz, Orts, Kadavath, Friedmann, Ghosh, Olsson, Chi, Pokharna, Güntert, Vögeli (bib30) 2020; 59 Lu, Hanes, Hunter (bib21) 1996; 380 Shapiro (bib2) August 2013 Karplus (bib12) 1963; 85 Prestegard, Al-Hashimi, Tolman (bib16) 2000; 33 Battiste, Wagner (bib13) 2000; 39 Bertini, Gupta, Luchinat, Parigi, Peana, Sgheri, Yuan (bib5) 2007; 129 Namanja, Wang, Xu, Mercedes-Camacho, Wilson, Etzkorn, Peng (bib23) 2011; 108 Jacobs, Saxena, Vogtherr, Bernadó, Pons, Fiebig (bib25) 2003; 278 Bernadó, Fernandes, Jacobs, Fiebig, García De La Torre, Pons (bib27) 2004; 29 Chi, Strotz, Riek, Vögeli (bib32) 2015; 62 Clore, Schwieters (bib19) 2004; 126 Ranganathan, Lu, Hunter, Noel (bib31) 1997; 89 Wriggers, Chakravarty, Jennings (bib1) 2005 Bouchard, Xia, Case, Peng (bib7) 2018; 430 Yaffe, Schutkowski, Shen, Zhou, Stukenberg, Rahfeld, Xu, Kuang, Kirschner, Fischer (bib22) 1997; 278 Bewley, Clore (bib3) 2000; 122 Vögeli, Güntert, Riek (bib18) 2013; 111 Bayer, Goettsch, Mueller, Griewel, Guiberman, Mayr, Bayer (bib26) 2003; 278 Vögeli (bib9) 2014; 78 Borbat, Georgieva, Freed (bib33) 2013; 4 Nichols, Born, Henen, Strotz, Orts, Olsson, Güntert, Chi, Vögeli (bib10) 2017; 22 Born, Soetbeer, Breitgoff, Henen, Sgourakis, Polyhach, Nichols, Strotz, Jeschke, Vögeli (bib8) 2021; 143 Ryabov, Fushman (bib6) 2007; 129 Fushman, Varadan, Assfalg, Walker (bib4) 2004; 44 Güntert (bib29) 2009; 38 Peng (bib28) 2015; 7 Nichols, Born, Henen, Strotz, Celestine, Güntert, Vögeli (bib11) 2018; 19 Losonczi, Andrec, Fischer, Prestegard (bib20) 1999; 138 Tolman, Ruan (bib17) 2006; 106 Tjandra, Bax (bib15) 1997; 278 Ranganathan, Lu, Hunter, Noel (bib24) 1997; 89 Clore (bib14) 2015; 564 Güntert (10.1016/j.mrl.2021.10.003_bib29) 2009; 38 Strotz (10.1016/j.mrl.2021.10.003_bib30) 2020; 59 Chi (10.1016/j.mrl.2021.10.003_bib32) 2015; 62 Nichols (10.1016/j.mrl.2021.10.003_bib10) 2017; 22 Fushman (10.1016/j.mrl.2021.10.003_bib4) 2004; 44 Bayer (10.1016/j.mrl.2021.10.003_bib26) 2003; 278 Peng (10.1016/j.mrl.2021.10.003_bib28) 2015; 7 Tolman (10.1016/j.mrl.2021.10.003_bib17) 2006; 106 Bewley (10.1016/j.mrl.2021.10.003_bib3) 2000; 122 Vögeli (10.1016/j.mrl.2021.10.003_bib18) 2013; 111 Bouchard (10.1016/j.mrl.2021.10.003_bib7) 2018; 430 Ranganathan (10.1016/j.mrl.2021.10.003_bib24) 1997; 89 Bernadó (10.1016/j.mrl.2021.10.003_bib27) 2004; 29 Clore (10.1016/j.mrl.2021.10.003_bib14) 2015; 564 Ryabov (10.1016/j.mrl.2021.10.003_bib6) 2007; 129 Borbat (10.1016/j.mrl.2021.10.003_bib33) 2013; 4 Shapiro (10.1016/j.mrl.2021.10.003_bib2) 2013 Vögeli (10.1016/j.mrl.2021.10.003_bib9) 2014; 78 Wriggers (10.1016/j.mrl.2021.10.003_bib1) 2005 Battiste (10.1016/j.mrl.2021.10.003_bib13) 2000; 39 Bertini (10.1016/j.mrl.2021.10.003_bib5) 2007; 129 Karplus (10.1016/j.mrl.2021.10.003_bib12) 1963; 85 Losonczi (10.1016/j.mrl.2021.10.003_bib20) 1999; 138 Namanja (10.1016/j.mrl.2021.10.003_bib23) 2011; 108 Nichols (10.1016/j.mrl.2021.10.003_bib11) 2018; 19 Prestegard (10.1016/j.mrl.2021.10.003_bib16) 2000; 33 Born (10.1016/j.mrl.2021.10.003_bib8) 2021; 143 Yaffe (10.1016/j.mrl.2021.10.003_bib22) 1997; 278 Jacobs (10.1016/j.mrl.2021.10.003_bib25) 2003; 278 Tjandra (10.1016/j.mrl.2021.10.003_bib15) 1997; 278 Ranganathan (10.1016/j.mrl.2021.10.003_bib31) 1997; 89 Clore (10.1016/j.mrl.2021.10.003_bib19) 2004; 126 Lu (10.1016/j.mrl.2021.10.003_bib21) 1996; 380 |
| References_xml | – volume: 122 start-page: 6009 year: 2000 end-page: 6016 ident: bib3 article-title: Determination of the relative orientation of the two halves of the domain-swapped dimer of cyanovirin-N in solution using dipolar couplings and rigid body minimization publication-title: J. Am. Chem. Soc. – volume: 44 start-page: 189 year: 2004 end-page: 214 ident: bib4 article-title: Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 129 start-page: 3315 year: 2007 end-page: 3327 ident: bib6 article-title: A model of interdomain mobility in a multidomain protein publication-title: J. Am. Chem. Soc. – volume: 129 start-page: 12786 year: 2007 end-page: 12794 ident: bib5 article-title: Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains publication-title: J. Am. Chem. Soc. – volume: 278 start-page: 1111 year: 1997 end-page: 1114 ident: bib15 article-title: Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium publication-title: Science – volume: 430 start-page: 2164 year: 2018 end-page: 2180 ident: bib7 article-title: Enhanced sampling of interdomain motion using map-restrained Langevin dynamics and NMR: application to Pin1 publication-title: J. Mol. Biol. – volume: 126 start-page: 2923 year: 2004 end-page: 2938 ident: bib19 publication-title: J. Am. Chem. Soc. – volume: 62 start-page: 63 year: 2015 end-page: 69 ident: bib32 article-title: Extending the ENOE data set of large proteins by evaluation of NOEs with unresolved diagonals publication-title: J. Biomol. NMR – volume: 106 start-page: 1720 year: 2006 end-page: 1736 ident: bib17 article-title: NMR residual dipolar couplings as probes of biomolecular dynamics publication-title: Chem. Rev. – volume: 22 start-page: 1176 year: 2017 ident: bib10 article-title: The exact nuclear overhauser enhancement: recent advances publication-title: Molecules – volume: 38 start-page: 129 year: 2009 end-page: 143 ident: bib29 article-title: Automated structure determination from NMR Spectra publication-title: Eur. Biophys. J. – volume: 59 start-page: 2 year: 2020 end-page: 10 ident: bib30 article-title: Protein allostery at atomic resolution publication-title: Angew. Chem. Int. Ed. – volume: 278 start-page: 26183 year: 2003 end-page: 26193 ident: bib26 article-title: Structural analysis of the mitotic regulator HPin1 in solution: insights into domain architecture and substrate binding publication-title: J. Biol. Chem. – volume: 564 start-page: 485 year: 2015 end-page: 497 ident: bib14 article-title: Practical aspects of paramagnetic relaxation enhancement in biological macromolecules publication-title: Methods Enzymol. – start-page: 736 year: 2005 end-page: 746 ident: bib1 article-title: Control of Protein Functional Dynamics by Peptide Linkers. – volume: 111 start-page: 437 year: 2013 end-page: 454 ident: bib18 article-title: Multiple-state ensemble structure determination from eNOE spectroscopy publication-title: Mol. Phys. – volume: 4 start-page: 170 year: 2013 end-page: 175 ident: bib33 article-title: Improved sensitivity for long-distance measurements in biomolecules: five-pulse double electron-electron resonance publication-title: J. Phys. Chem. Lett. – start-page: 58 year: August 2013 end-page: 117 ident: bib2 article-title: NMR spectroscopy on domain dynamics in biomacromolecules publication-title: Prog. Biophys. Mol. Biol. – volume: 278 start-page: 1957 year: 1997 end-page: 1960 ident: bib22 article-title: Sequence-specific and phosphorylation dependent proline isomerization: a potential mitotic regulatory mechanism publication-title: Science (80-. ) – volume: 39 start-page: 5879 year: 2000 end-page: 5896 ident: bib13 article-title: Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data publication-title: Biochemistry – volume: 89 start-page: 875 year: 1997 end-page: 886 ident: bib24 article-title: Structural and functional analysis of the mitotic rotamase Pin1 suggest substrate recognition is phosphorylation dependent publication-title: Cell – volume: 143 start-page: 16055 year: 2021 end-page: 16067 ident: bib8 article-title: Reconstruction of coupled intra- and interdomain protein motion from nuclear and electron magnetic resonance publication-title: J. Am. Chem. Soc. – volume: 89 start-page: 875 year: 1997 end-page: 886 ident: bib31 article-title: Structural and functional analysis of the mitotic rotamase Pin1 suggest substrate recognition is phosphorylation dependent publication-title: Cell – volume: 85 start-page: 2870 year: 1963 end-page: 2871 ident: bib12 publication-title: J. Am. Chem. Soc. – volume: 108 start-page: 12289 year: 2011 end-page: 12294 ident: bib23 article-title: Stereospecific gating of functional motions in Pin1 publication-title: Proc. Natl. Acad. Sci. – volume: 19 start-page: 1695 year: 2018 end-page: 1701 ident: bib11 article-title: Extending the applicability of exact nuclear overhauser enhancements to large proteins and RNA publication-title: Chembiochem – volume: 29 start-page: 21 year: 2004 end-page: 35 ident: bib27 article-title: Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on brownian dynamic simulations publication-title: J. Biomol. NMR – volume: 7 start-page: 239 year: 2015 end-page: 249 ident: bib28 article-title: Investigating dynamic interdomain allostery in Pin1 publication-title: Biophys. Rev. – volume: 138 start-page: 334 year: 1999 end-page: 342 ident: bib20 article-title: Order matrix analysis of residual dipolar couplings using singular value decomposition publication-title: J. Magn. Reson. – volume: 380 start-page: 544 year: 1996 end-page: 547 ident: bib21 article-title: A human peptidyl-prolyl isomerase essential for regulation of mitosis publication-title: Nature – volume: 278 start-page: 26174 year: 2003 end-page: 26182 ident: bib25 article-title: Peptide binding induces large scale changes in inter-domain mobility in human Pin1 publication-title: J. Biol. Chem. – volume: 78 start-page: 1 year: 2014 end-page: 46 ident: bib9 article-title: The nuclear overhauser effect from a quantitative perspective publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 33 start-page: 371 year: 2000 end-page: 424 ident: bib16 article-title: NMR structures of biomolecules using field oriented media and residual dipolar couplings publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 44 start-page: 189 year: 2004 ident: 10.1016/j.mrl.2021.10.003_bib4 article-title: Determining domain orientation in macromolecules by using spin-relaxation and residual dipolar coupling measurements publication-title: Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/j.pnmrs.2004.02.001 – start-page: 58 year: 2013 ident: 10.1016/j.mrl.2021.10.003_bib2 article-title: NMR spectroscopy on domain dynamics in biomacromolecules publication-title: Prog. Biophys. Mol. Biol. doi: 10.1016/j.pbiomolbio.2013.05.001 – volume: 278 start-page: 1957 issue: 5345 year: 1997 ident: 10.1016/j.mrl.2021.10.003_bib22 article-title: Sequence-specific and phosphorylation dependent proline isomerization: a potential mitotic regulatory mechanism publication-title: Science (80-. ) doi: 10.1126/science.278.5345.1957 – volume: 22 start-page: 1176 year: 2017 ident: 10.1016/j.mrl.2021.10.003_bib10 article-title: The exact nuclear overhauser enhancement: recent advances publication-title: Molecules doi: 10.3390/molecules22071176 – volume: 78 start-page: 1 year: 2014 ident: 10.1016/j.mrl.2021.10.003_bib9 article-title: The nuclear overhauser effect from a quantitative perspective publication-title: Prog. Nucl. Magn. Reson. Spectrosc. doi: 10.1016/j.pnmrs.2013.11.001 – volume: 143 start-page: 16055 year: 2021 ident: 10.1016/j.mrl.2021.10.003_bib8 article-title: Reconstruction of coupled intra- and interdomain protein motion from nuclear and electron magnetic resonance publication-title: J. Am. Chem. Soc. doi: 10.1021/jacs.1c06289 – volume: 380 start-page: 544 issue: 6574 year: 1996 ident: 10.1016/j.mrl.2021.10.003_bib21 article-title: A human peptidyl-prolyl isomerase essential for regulation of mitosis publication-title: Nature doi: 10.1038/380544a0 – volume: 33 start-page: 371 year: 2000 ident: 10.1016/j.mrl.2021.10.003_bib16 article-title: NMR structures of biomolecules using field oriented media and residual dipolar couplings publication-title: Prog. Nucl. Magn. Reson. Spectrosc. – volume: 138 start-page: 334 year: 1999 ident: 10.1016/j.mrl.2021.10.003_bib20 article-title: Order matrix analysis of residual dipolar couplings using singular value decomposition publication-title: J. Magn. Reson. doi: 10.1006/jmre.1999.1754 – volume: 111 start-page: 437 year: 2013 ident: 10.1016/j.mrl.2021.10.003_bib18 article-title: Multiple-state ensemble structure determination from eNOE spectroscopy publication-title: Mol. Phys. doi: 10.1080/00268976.2012.728257 – volume: 126 start-page: 2923 year: 2004 ident: 10.1016/j.mrl.2021.10.003_bib19 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0386804 – volume: 129 start-page: 3315 year: 2007 ident: 10.1016/j.mrl.2021.10.003_bib6 article-title: A model of interdomain mobility in a multidomain protein publication-title: J. Am. Chem. Soc. doi: 10.1021/ja067667r – volume: 564 start-page: 485 year: 2015 ident: 10.1016/j.mrl.2021.10.003_bib14 article-title: Practical aspects of paramagnetic relaxation enhancement in biological macromolecules publication-title: Methods Enzymol. doi: 10.1016/bs.mie.2015.06.032 – volume: 278 start-page: 1111 year: 1997 ident: 10.1016/j.mrl.2021.10.003_bib15 article-title: Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium publication-title: Science doi: 10.1126/science.278.5340.1111 – volume: 278 start-page: 26174 issue: 28 year: 2003 ident: 10.1016/j.mrl.2021.10.003_bib25 article-title: Peptide binding induces large scale changes in inter-domain mobility in human Pin1 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M300796200 – volume: 39 start-page: 5879 year: 2000 ident: 10.1016/j.mrl.2021.10.003_bib13 article-title: Utilization of site-directed spin labeling and high-resolution heteronuclear nuclear magnetic resonance for global fold determination of large proteins with limited nuclear overhauser effect data publication-title: Biochemistry doi: 10.1021/bi000060h – volume: 19 start-page: 1695 year: 2018 ident: 10.1016/j.mrl.2021.10.003_bib11 article-title: Extending the applicability of exact nuclear overhauser enhancements to large proteins and RNA publication-title: Chembiochem doi: 10.1002/cbic.201800237 – volume: 38 start-page: 129 year: 2009 ident: 10.1016/j.mrl.2021.10.003_bib29 article-title: Automated structure determination from NMR Spectra publication-title: Eur. Biophys. J. doi: 10.1007/s00249-008-0367-z – volume: 4 start-page: 170 year: 2013 ident: 10.1016/j.mrl.2021.10.003_bib33 article-title: Improved sensitivity for long-distance measurements in biomolecules: five-pulse double electron-electron resonance publication-title: J. Phys. Chem. Lett. doi: 10.1021/jz301788n – start-page: 736 year: 2005 ident: 10.1016/j.mrl.2021.10.003_bib1 – volume: 29 start-page: 21 year: 2004 ident: 10.1016/j.mrl.2021.10.003_bib27 article-title: Interpretation of NMR relaxation properties of Pin1, a two-domain protein, based on brownian dynamic simulations publication-title: J. Biomol. NMR doi: 10.1023/B:JNMR.0000019499.60777.6e – volume: 89 start-page: 875 year: 1997 ident: 10.1016/j.mrl.2021.10.003_bib31 article-title: Structural and functional analysis of the mitotic rotamase Pin1 suggest substrate recognition is phosphorylation dependent publication-title: Cell doi: 10.1016/S0092-8674(00)80273-1 – volume: 85 start-page: 2870 year: 1963 ident: 10.1016/j.mrl.2021.10.003_bib12 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja00901a059 – volume: 430 start-page: 2164 year: 2018 ident: 10.1016/j.mrl.2021.10.003_bib7 article-title: Enhanced sampling of interdomain motion using map-restrained Langevin dynamics and NMR: application to Pin1 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2018.05.007 – volume: 59 start-page: 2 year: 2020 ident: 10.1016/j.mrl.2021.10.003_bib30 article-title: Protein allostery at atomic resolution publication-title: Angew. Chem. Int. Ed. doi: 10.1002/anie.202008734 – volume: 108 start-page: 12289 issue: 30 year: 2011 ident: 10.1016/j.mrl.2021.10.003_bib23 article-title: Stereospecific gating of functional motions in Pin1 publication-title: Proc. Natl. Acad. Sci. doi: 10.1073/pnas.1019382108 – volume: 122 start-page: 6009 year: 2000 ident: 10.1016/j.mrl.2021.10.003_bib3 article-title: Determination of the relative orientation of the two halves of the domain-swapped dimer of cyanovirin-N in solution using dipolar couplings and rigid body minimization publication-title: J. Am. Chem. Soc. doi: 10.1021/ja000858o – volume: 62 start-page: 63 issue: 1 year: 2015 ident: 10.1016/j.mrl.2021.10.003_bib32 article-title: Extending the ENOE data set of large proteins by evaluation of NOEs with unresolved diagonals publication-title: J. Biomol. NMR doi: 10.1007/s10858-015-9917-8 – volume: 89 start-page: 875 year: 1997 ident: 10.1016/j.mrl.2021.10.003_bib24 article-title: Structural and functional analysis of the mitotic rotamase Pin1 suggest substrate recognition is phosphorylation dependent publication-title: Cell doi: 10.1016/S0092-8674(00)80273-1 – volume: 106 start-page: 1720 year: 2006 ident: 10.1016/j.mrl.2021.10.003_bib17 article-title: NMR residual dipolar couplings as probes of biomolecular dynamics publication-title: Chem. Rev. doi: 10.1021/cr040429z – volume: 278 start-page: 26183 year: 2003 ident: 10.1016/j.mrl.2021.10.003_bib26 article-title: Structural analysis of the mitotic regulator HPin1 in solution: insights into domain architecture and substrate binding publication-title: J. Biol. Chem. doi: 10.1074/jbc.M300721200 – volume: 7 start-page: 239 issue: 2 year: 2015 ident: 10.1016/j.mrl.2021.10.003_bib28 article-title: Investigating dynamic interdomain allostery in Pin1 publication-title: Biophys. Rev. doi: 10.1007/s12551-015-0171-9 – volume: 129 start-page: 12786 year: 2007 ident: 10.1016/j.mrl.2021.10.003_bib5 article-title: Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains publication-title: J. Am. Chem. Soc. doi: 10.1021/ja0726613 |
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| Title | On the use of residual dipolar couplings in multi-state structure calculation of two-domain proteins |
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