Related Articles3D NMR spectroscopy for resonance assignment and structure elucidation of proteins under MAS: novel pulse schemes and sensitivity considerations.
J Magn Reson. 2005 Mar;173(1):64-74
Authors: Heise H, Seidel K, Etzkorn M, Becker S, Baldus M
Two types of 3D MAS NMR experiments are introduced, which combine standard (NC,CC) transfer schemes with (1H,1H) mixing to simultaneously detect connectivities and structural constraints of uniformly 15N,13C-labeled proteins with high spectral resolution. The homonuclear CCHHC and CCC experiments are recorded with one double-quantum evolution dimension in order to avoid a cubic diagonal in the spectrum. Depending on the second transfer step, spin systems or proton-proton contacts can be determined with reduced spectral overlap. The heteronuclear NHHCC experiment encodes NH-HC proton-proton interactions, which are indicative for the backbone conformation of the protein. The third dimension facilitates the identification of the amino acid spin system. Experimental results on U-[15N,13C]valine and U-[15N,13C]ubiquitin demonstrate their usefulness for resonance assignments and for the determination of structural constraints. Furthermore, we give a detailed analysis of alternative multidimensional sampling schemes and their effect on sensitivity and resolution.
Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins
Rapid measurement of residual dipolar couplings for fast fold elucidation of proteins
Abstract It has been demonstrated that protein folds can be determined using appropriate computational protocols with NMR chemical shifts as the sole source of experimental restraints. While such approaches are very promising they still suffer from low convergence resulting in long computation times to achieve accurate results. Here we present a suite of time- and sensitivity optimized NMR experiments for rapid measurement of up to six RDCs per residue. Including such an RDC data set, measured in less...
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Exclusively NOESY-based automated NMR assignment and structure determination of proteins
Exclusively NOESY-based automated NMR assignment and structure determination of proteins
Abstract A fully automated method is presented for determining NMR solution structures of proteins using exclusively NOESY spectra as input, obviating the need to measure any spectra only for obtaining resonance assignments but devoid of structural information. Applied to two small proteins, the approach yielded structures that coincided closely with conventionally determined structures.
Content Type Journal Article
Pages 1-10
DOI 10.1007/s10858-011-9502-8
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04-01-2011 09:31 PM
Exclusively NOESY-based automated NMR assignment and structure determination of proteins.
Exclusively NOESY-based automated NMR assignment and structure determination of proteins.
Exclusively NOESY-based automated NMR assignment and structure determination of proteins.
J Biomol NMR. 2011 Mar 30;
Authors: Ikeya T, Jee JG, Shigemitsu Y, Hamatsu J, Mishima M, Ito Y, Kainosho M, Güntert P
A fully automated method is presented for determining NMR solution structures of proteins using exclusively NOESY spectra as input, obviating the need to measure any spectra only for obtaining resonance assignments but devoid of structural information....
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03-31-2011 06:24 PM
Towards fully automated structure-based NMR resonance assignment of (15)n-labeled proteins from automatically picked peaks.
Towards fully automated structure-based NMR resonance assignment of (15)n-labeled proteins from automatically picked peaks.
Towards fully automated structure-based NMR resonance assignment of (15)n-labeled proteins from automatically picked peaks.
J Comput Biol. 2011 Mar;18(3):347-63
Authors: Jang R, Gao X, Li M
Abstract In NMR resonance assignment, an indispensable step in NMR protein studies, manually processed peaks from both N-labeled and C-labeled spectra are typically used as inputs. However, the use of homologous structures can allow...
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03-10-2011 03:51 PM
[NMR paper] NMR resonance assignment of selectively labeled proteins by the use of paramagnetic l
NMR resonance assignment of selectively labeled proteins by the use of paramagnetic ligands.
Related Articles NMR resonance assignment of selectively labeled proteins by the use of paramagnetic ligands.
J Biomol NMR. 2004 Oct;30(2):205-10
Authors: Cutting B, Strauss A, Fendrich G, Manley PW, Jahnke W
Selective isotopic labeling of larger proteins greatly simplifies protein NMR spectra and reduces signal overlap, but selectively labeled proteins cannot be easily assigned since the sequential assignment method is not applicable. Here we describe...
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11-24-2010 10:01 PM
[NMR paper] Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional
Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR.
Related Articles Resonance assignment of 13C/15N labeled solid proteins by two- and three-dimensional magic-angle-spinning NMR.
J Biomol NMR. 1999 Sep;15(1):1-14
Authors: Hong M
The comprehensive structure determination of isotopically labeled proteins by solid-state NMR requires sequence-specific assignment of 13C and 15N spectra. We describe several 2D and 3D MAS correlation techniques for resonance assignment and apply them, at 7.0...
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11-18-2010 08:31 PM
[NMR paper] Resonance assignment strategies for the analysis of NMR spectra of proteins.
Resonance assignment strategies for the analysis of NMR spectra of proteins.
Related Articles Resonance assignment strategies for the analysis of NMR spectra of proteins.
Mol Biotechnol. 1994 Aug;2(1):61-93
Authors: Leopold MF, Urbauer JL, Wand AJ
Determination of the high resolution solution structure of a protein using nuclear magnetic resonance (NMR) spectroscopy requires that resonances observed in the NMR spectra be unequivocally assigned to individual nuclei of the protein. With the advent of modern, two-dimensional NMR techniques arose...
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[NMR paper] Assignment of the 1H NMR spectrum and secondary structure elucidation of the single-s
Assignment of the 1H NMR spectrum and secondary structure elucidation of the single-stranded DNA binding protein encoded by the filamentous bacteriophage IKe.
Related Articles Assignment of the 1H NMR spectrum and secondary structure elucidation of the single-stranded DNA binding protein encoded by the filamentous bacteriophage IKe.
Biochemistry. 1992 Feb 4;31(4):1254-62
Authors: van Duynhoven JP, Folkers PJ, Prinse CW, Harmsen BJ, Konings RN, Hilbers CW
By means of 2D NMR techniques, all backbone resonances in the 1H NMR spectrum of the...
3D NMR spectroscopy for resonance assignment and structure elucidation of proteins un
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