Resolution Enhancement by Homonuclear J-decoupling: Application to Three-dimensional Solid-state Magic Angle Spinning NMR Spectroscopy

Overview

Journal J Biomol NMR

Publisher Springer

Specialties Molecular Biology
Nuclear Medicine

Date 2008 Apr 12

PMID 18404253

Citations 5

Authors

Lichi Shi

Xiaohu Peng

Mumdooh A M Ahmed

Dale Edwards

Leonid S Brown

Vladimir Ladizhansky

Affiliations

Soon will be listed here.

Abstract

We describe a simple protocol to achieve homonuclear J-decoupling in the indirect dimensions of multidimensional experiments, and to enhance spectral resolution of the backbone Calpha carbons in the 3D NCACX experiment. In the proposed protocol, the refocusing of the Calpha-CO homonuclear J-couplings is achieved by applying an off-resonance selective pi pulse to the CO spectral region in the middle of Calpha chemical shift evolution. As is commonly used in solution NMR, a compensatory echo period is used to refocus the unwanted chemical shift evolution of Calpha spins, which takes place during the off-resonance selective pulse. The experiments were carried out on the beta1 immunoglobulin binding domain of protein G (GB1). In GB1, such implementation results in significantly reduced line widths, and leads to an overall sensitivity enhancement.

Citing Articles

Biomaterial Property Effects on Platelets and Macrophages: An in Vitro Study.

Fernandes K, Zhang Y, Magri A, Renno A, van den Beucken J ACS Biomater Sci Eng. 2017; 3(12):3318-3327.

PMID: 29250594 PMC: 5727470. DOI: 10.1021/acsbiomaterials.7b00679.

Lipid bilayer-bound conformation of an integral membrane beta barrel protein by multidimensional MAS NMR.

Eddy M, Su Y, Silvers R, Andreas L, Clark L, Wagner G J Biomol NMR. 2015; 61(3-4):299-310.

PMID: 25634301 PMC: 4398622. DOI: 10.1007/s10858-015-9903-1.

Long-observation-window band-selective homonuclear decoupling: increased sensitivity and resolution in solid-state NMR spectroscopy of proteins.

Struppe J, Yang C, Wang Y, Hernandez R, Shamansky L, Mueller L J Magn Reson. 2013; 236:89-94.

PMID: 24095840 PMC: 4017862. DOI: 10.1016/j.jmr.2013.09.001.

Optimal degree of protonation for ¹H detection of aliphatic sites in randomly deuterated proteins as a function of the MAS frequency.

Asami S, Szekely K, Schanda P, Meier B, Reif B J Biomol NMR. 2012; 54(2):155-68.

PMID: 22915373 DOI: 10.1007/s10858-012-9659-9.

Targeted 13C-13C distance measurements in a microcrystalline protein via J-decoupled rotational resonance width measurements.

van der Wel P, Eddy M, Ramachandran R, Griffin R Chemphyschem. 2009; 10(9-10):1656-63.

PMID: 19565580 PMC: 4440578. DOI: 10.1002/cphc.200900102.

References

Morcombe C, Zilm K . Chemical shift referencing in MAS solid state NMR. J Magn Reson. 2003; 162(2):479-86. DOI: 10.1016/s1090-7807(03)00082-x. View

Markley J, Bax A, Arata Y, Hilbers C, Kaptein R, Sykes B . Recommendations for the presentation of NMR structures of proteins and nucleic acids--IUPAC-IUBMB-IUPAB Inter-Union Task Group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy. Eur J Biochem. 1998; 256(1):1-15. DOI: 10.1046/j.1432-1327.1998.2560001.x. View

Duma L, Hediger S, Brutscher B, Bockmann A, Emsley L . Resolution enhancement in multidimensional solid-state NMR spectroscopy of proteins using spin-state selection. J Am Chem Soc. 2003; 125(39):11816-7. DOI: 10.1021/ja036893n. View

Delaglio F, Grzesiek S, Vuister G, Zhu G, Pfeifer J, Bax A . NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995; 6(3):277-93. DOI: 10.1007/BF00197809. View

Igumenova T, McDermott A . Homo-nuclear 13C J-decoupling in uniformly 13C-enriched solid proteins. J Magn Reson. 2005; 175(1):11-20. DOI: 10.1016/j.jmr.2005.03.007. View

Igumenova T, McDermott A . Improvement of resolution in solid state NMR spectra with J-decoupling: an analysis of lineshape contributions in uniformly 13C-enriched amino acids and proteins. J Magn Reson. 2003; 164(2):270-85. DOI: 10.1016/s1090-7807(03)00239-8. View

Franks W, Zhou D, Wylie B, Money B, Graesser D, Frericks H . Magic-angle spinning solid-state NMR spectroscopy of the beta1 immunoglobulin binding domain of protein G (GB1): 15N and 13C chemical shift assignments and conformational analysis. J Am Chem Soc. 2005; 127(35):12291-305. DOI: 10.1021/ja044497e. View

Hong M . Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR. J Biomol NMR. 1999; 15(1):1-14. DOI: 10.1023/a:1008334204412. View

Siemer A, Ritter C, Ernst M, Riek R, Meier B . High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation. Angew Chem Int Ed Engl. 2005; 44(16):2441-4. DOI: 10.1002/anie.200462952. View

10.

Zhou D, Kloepper K, Winter K, Rienstra C . Band-selective 13C homonuclear 3D spectroscopy for solid proteins at high field with rotor-synchronized soft pulses. J Biomol NMR. 2006; 34(4):245-57. DOI: 10.1007/s10858-006-0026-6. View

11.

Duma L, Hediger S, Lesage A, Emsley L . Spin-state selection in solid-state NMR. J Magn Reson. 2003; 164(1):187-95. DOI: 10.1016/s1090-7807(03)00187-3. View

12.

Duma L, Hediger S, Lesage A, Sakellariou D, Emsley L . Carbon-13 lineshapes in solid-state NMR of labeled compounds. Effects of coherent CSA-dipolar cross-correlation. J Magn Reson. 2003; 162(1):90-101. DOI: 10.1016/s1090-7807(02)00174-x. View

13.

Straus S, Bremi T, Ernst R . Experiments and strategies for the assignment of fully 13C/15N-labelled polypeptides by solid state NMR. J Biomol NMR. 1998; 12(1):39-50. DOI: 10.1023/a:1008280716360. View

14.

Hiller M, Krabben L, Vinothkumar K, Castellani F, van Rossum B, Kuhlbrandt W . Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli. Chembiochem. 2005; 6(9):1679-84. DOI: 10.1002/cbic.200500132. View

15.

Li Y, Wylie B, Rienstra C . Selective refocusing pulses in magic-angle spinning NMR: characterization and applications to multi-dimensional protein spectroscopy. J Magn Reson. 2006; 179(2):206-16. DOI: 10.1016/j.jmr.2005.12.003. View

16.

Jaroniec C, MacPhee C, Astrof N, Dobson C, Griffin R . Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril. Proc Natl Acad Sci U S A. 2002; 99(26):16748-53. PMC: 139215. DOI: 10.1073/pnas.252625999. View

17.

Frericks Schmidt H, Sperling L, Gao Y, Wylie B, Boettcher J, Wilson S . Crystal polymorphism of protein GB1 examined by solid-state NMR spectroscopy and X-ray diffraction. J Phys Chem B. 2007; 111(51):14362-9. PMC: 2774121. DOI: 10.1021/jp075531p. View

18.

Paravastu A, Petkova A, Tycko R . Polymorphic fibril formation by residues 10-40 of the Alzheimer's beta-amyloid peptide. Biophys J. 2006; 90(12):4618-29. PMC: 1471876. DOI: 10.1529/biophysj.105.076927. View

19.

Chevelkov V, Chen Z, Bermel W, Reif B . Resolution enhancement in MAS solid-state NMR by application of 13C homonuclear scalar decoupling during acquisition. J Magn Reson. 2004; 172(1):56-62. DOI: 10.1016/j.jmr.2004.09.017. View

20.

Zhong L, Bamm V, Ahmed M, Harauz G, Ladizhansky V . Solid-state NMR spectroscopy of 18.5 kDa myelin basic protein reconstituted with lipid vesicles: spectroscopic characterisation and spectral assignments of solvent-exposed protein fragments. Biochim Biophys Acta. 2007; 1768(12):3193-205. PMC: 3525669. DOI: 10.1016/j.bbamem.2007.08.013. View