An R1ρ expression for a spin in chemical exchange between two sites with unequal transverse relaxation rates

Journal of Biomolecular NMR

Volumn 55, Issue 2, 2013, Pages 211-218

  Baldwin, Andrew J ^a,c   Kay, Lewis E ^a,b  

^a UNIVERSITY OF TORONTO   (Canada)

^b HOSPITAL FOR SICK CHILDREN   (Canada)

^c UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

Differential transverse relaxation; Invisible excited states; Protein conformational exchange; Relaxation dispersion NMR; Rotating frame relaxation; Spin lock

Indexed keywords

ACCELERATION; ARTICLE; CONFORMATIONAL TRANSITION; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PARAMETERS; PRIORITY JOURNAL; RELAXATION RATE;

MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION;

EID: 84879552012     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-012-9694-6     Document Type: Article

References (43)

1. Allerhand A, Thiele E (1966) Analysis of Carr-Prucell spinecho NMR experiments on multiple spin systems. II. The effect of chemical exchange. J Chem Phys 45:902-916
2. Allerhand A, Gutowsky HS, Jonas J, Meinzer RA (1966) Nuclear magnetic resonance methods for determining chemical-exchange rates. J Am Chem Soc 88:3185-3194
3. Anet FA, Basus VJ (1978) Limiting equations for exchanging broadening in 2-site NMR systems with very unequal populations. J Magn Reson 32:339-343
4. Auer R, Neudecker P, Muhandiram DR, Lundstrom P, Hansen DF, Konrat R, Kay LE (2009) Measuring the signs of 1H(alpha) chemical shift differences between ground and excited protein states by off-resonance spin-lock R(1rho) NMR spectroscopy. J Am Chem Soc 131:10832-10833
5. Auer R, Hansen DF, Neudecker P, Korzhnev DM, Muhandiram DR, Konrat R, Kay LE (2010) Measurement of signs of chemical shift differences between ground and excited protein states: a comparison between H(S/M)QC and R1rho methods. J Biomol NMR 46:205-216
6. Baldwin AJ, Kay LE (2012) Measurement of the signs of methyl 13C chemical shift differences between interconverting ground and excited protein states by R1rho: an application to aB crystallin. J Biomol NMR 53:1-12
7. Baldwin AJ, Hilton GR, Lioe H, Bagneris C, Benesch JL, Kay LE (2011a) Quaternary dynamics of alpha B-crystallin as a direct consequence of localised tertiary fluctuations in the C-terminus. J Mol Biol 413:310-320
8. Baldwin AJ, Lioe H, Robinson CV, Kay LE, Benesch JL (2011b) AlphaB-crystallin polydispersity is a consequence of unbiased quaternary dynamics. J Mol Biol 413:297-309
9. Baldwin AJ, Walsh P, Hansen DF, Hilton GR, Benesch JL, Sharpe S, Kay LE (2012) Probing dynamic conformations of the high molecular weight aB-crystallin heat shock protein ensemble by NMR spectroscopy. J Am Chem Soc 134:15343-15350
10. Boehr DD, McElheny D, Dyson HJ, Wright PE (2006) The dynamic energy landscape of dihydrofolate reductase catalysis. Science 313:1638-1642
11. Carver JP, Richards RE (1972) A general two-site solution for the chemical exchange produced dependence of T2 upon the Carr-Purcell pulse separation. J Magn Reson 6:89-105
12. Deverell C, Morgan RE, Strange JH (1970) Studies of chemical exchange by nuclear magnetic relaxation in the rotating frame. Mol Phys 18:553-559
13. Fiaux J, Bertelsen EB, Horwich AL, Wüthrich K (2002) NMR analysis of a 900K GroEL GroES complex. Nature 418:207-211
14. Fraser JS, Clarkson MW, Degnan SC, Erion R, Kern D, Alber T (2009) Hidden alternative structures of proline isomerase essential for catalysis. Nature 462:669-673
15. Hansen DF, Vallurupalli P, Kay LE (2008) Using relaxation dispersion NMR spectroscopy to determine structures of excited, invisible protein states. J Biomol NMR 41:113-120
16. Henzler-Wildman K, Kern D (2007) Dynamic personalities of proteins. Nature 450:964-972
17. Ishima R, Torchia DA (1999) Estimating the time scale of chemical exchange of proteins from measurements of transverse relaxation rates in solution. J Biomol NMR 14:369-372
18. Ishima R, Torchia DA (2000) Protein dynamics from NMR. Nat Struct Biol 7:740-743
19. 0B. J Biomol NMR 34:209-219
20. Ishima R, Freedberg DI, Wang YX, Louis JM, Torchia DA (1999) Flap opening and dimer-interface flexibility in the free and inhibitor- bound HIV protease, and their implications for function. Struct Fold Des 7:1047-1055
21. Iwahara J, Clore GM (2006) Detecting transient intermediates in macromolecular binding by paramagnetic NMR. Nature 440:1227-1230
22. Jen J (1978) Chemical exchange and NMR T2 relaxation - multisite case. J Magn Reson 30:111-128
23. Karplus M, Kuriyan J (2005) Molecular dynamics and protein function. Proc Natl Acad Sci USA 102:6679-6685
24. Korzhnev DM, Kay LE (2008) Probing invisible, low-populated States of protein molecules by relaxation dispersion NMR spectroscopy: an application to protein folding. Acc Chem Res 41:442-451
25. Korzhnev DM, Orekhov VY, Dahlquist FW, Kay LE (2003) Off-resonance R1rho relaxation outside of the fast exchange limit: an experimental study of a cavity mutant of T4 lysozyme. J Biomol NMR 26:39-48
26. Korzhnev DM, Salvatella X, Vendruscolo M, Di Nardo AA, Davidson AR, Dobson CM, Kay LE (2004) Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR. Nature 430:586-590
27. Korzhnev DM, Orekhov VY, Kay LE (2005) Off-resonance R(1rho) NMR studies of exchange dynamics in proteins with low spin-lock fields: an application to a Fyn SH3 domain. J Am Chem Soc 127:713-721
28. Korzhnev DM, Religa TL, Banachewicz W, Fersht AR, Kay LE (2010) A transient and low-populated protein-folding intermediate at atomic resolution. Science 329:1312-1316
29. Lange OF, Lakomek NA, Fares C, Schroder GF, Walter KF, Becker S, Meiler J, Grubmuller H, Griesinger C, de Groot BL (2008) Recognition dynamics up to microseconds revealed from an RDC-derived ubiquitin ensemble in solution. Science 320:1471-1475
30. Lindorff-Larsen K, Best RB, Depristo MA, Dobson CM, Vendruscolo M (2005) Simultaneous determination of protein structure and dynamics. Nature 433:128-132
31. Luz Z, Meiboom S (1963) Nuclear magnetic resonance study of protolysis of trimethylammonium ion in aqueous solution-order of reaction with respect to solvent. J Chem Phys 39:366-370
32. McConnell HM (1958) Reaction rates by nuclear magnetic resonance. J Chem Phys 28:430-431
33. Miloushev VZ, Palmer AG 3rd (2005) R(1rho) relaxation for two-site chemical exchange: general approximations and some exact solutions. J Magn Reson 177:221-227
34. Mittermaier A, Kay LE (2006) New tools provide new insights in NMR studies of protein dynamics. Science 312:224-228
35. Palmer AG, Massi F (2006) Characterization of the dynamics of biomacromolecules using rotating-frame spin relaxation NMR spectroscopy. Chem Rev 106:1700-1719
36. Palmer AG, Williams J, McDermott A (1996) Nuclear magnetic resonance studies of biopolymer dynamics. J Phys Chem 100:13293-13310
37. Palmer AG, Kroenke CD, Loria JP (2001) NMR methods for quantifying microsecond-to-millisecond motions in biological macromolecules. Methods Enzymol 339:204-238
38. Palmer AG, Grey MJ, Wang C (2005) Solution NMR spin relaxation methods for characterizing chemical exchange in high-molecular-weight systems. Methods Enzymol 394:430-465
39. Skrynnikov NR, Dahlquist FW, Kay LE (2002) Reconstructing NMR spectra of "invisible" excited protein states using HSQC and HMQC experiments. J Am Chem Soc 124:12352-12360
40. Sprangers R, Kay LE (2007) Quantitative dynamic and binding studies of the 20S proteasome by NMR. Nature 445:618-622
41. Sugase K, Dyson HJ, Wright PE (2007) Mechanism of coupled folding and binding of an intrinsically disordered protein. Nature 447:1021-1024
42. Tang C, Schwieters CD, Clore GM (2007) Open-to-closed transition in apo maltose-binding protein observed by paramagnetic NMR. Nature 449:1078-1082
43. Trott O, Palmer AG 3rd (2002) R1rho relaxation outside of the fast-exchange limit. J Magn Reson 154:157-160