Related ArticlesComplete resonance assignment for the polypeptide backbone of interleukin 1 beta using three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1990 Apr 10;29(14):3542-56
Authors: Driscoll PC, Clore GM, Marion D, Wingfield PT, Gronenborn AM
The complete sequence-specific assignment of the 15N and 1H backbone resonances of the NMR spectrum of recombinant human interleukin 1 beta (153 residues, Mr = 17,400) has been obtained by using primarily 15N-1H heteronuclear three-dimensional (3D) NMR techniques in combination with 15N-1H heteronuclear and 1H homonuclear two-dimensional NMR. The fingerprint region of the spectrum was analyzed by using a combination of 3D heteronuclear 1H Hartmann-Hahn 15N-1H multiple quantum coherence (3D HOHAHA-HMQC) and 3D heteronuclear 1H nuclear Overhauser 15N-1H multiple quantum coherence (3D NOESY-HMQC) spectroscopies. We show that the problems of amide NH and C alpha H chemical shift degeneracy that are prevalent for proteins of this size are readily overcome by using the 3D heteronuclear NMR technique. A doubling of some peaks in the spectrum was found to be due to N-terminal heterogeneity of the 15N-labeled protein, corresponding to a mixture of wild-type and des-Ala-1-interleukin 1 beta. The complete list of 15N and 1H assignments is given for all the amide NH and C alpha H resonances of all non-proline residues, as well as the 1H assignments for some of the amino acid side chains. This first example of the sequence-specific assignment of a protein using heteronuclear 3D NMR provides a basis for further conformational and dynamic studies of interleukin 1 beta.
[NMR paper] Reconsidering complete search algorithms for protein backbone NMR assignment.
Reconsidering complete search algorithms for protein backbone NMR assignment.
Related Articles Reconsidering complete search algorithms for protein backbone NMR assignment.
Bioinformatics. 2005 Sep 1;21 Suppl 2:ii230-6
Authors: Vitek O, Bailey-Kellogg C, Craig B, Kuliniewicz P, Vitek J
MOTIVATION: Nuclear magnetic resonance (NMR) spectroscopy is widely used to determine and analyze protein structures. An essential step in NMR studies is determining the backbone resonance assignment, which maps individual atoms to experimentally measured...
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[NMR paper] G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment
G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment.
Related Articles G-matrix Fourier transform NMR spectroscopy for complete protein resonance assignment.
Proc Natl Acad Sci U S A. 2004 Jun 29;101(26):9642-7
Authors: Atreya HS, Szyperski T
A G-matrix Fourier transform (GFT) NMR spectroscopy-based strategy for resonance assignment of proteins is described. Each of the GFT NMR experiments presented here rapidly affords four-, five-, or six-dimensional spectral information in combination with precise...
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[NMR paper] Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues
Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin.
Related Articles Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin.
J Biomol NMR. 1992 Nov;2(6):597-618
Authors: Qin J, La Mar GN
Two-dimensional sequence-specific 1H NMR resonance assignment methodology (Wüthrich, 1986) has been applied for the first...
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[NMR paper] Polypeptide backbone resonance assignments and secondary structure of Bacillus subtil
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Related Articles Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1991 Jul 16;30(28):6896-907
Authors: Fairbrother WJ, Cavanagh J, Dyson HJ, Palmer AG, Sutrina SL, Reizer J, Saier MH, Wright PE
The enzyme...
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[NMR paper] Polypeptide backbone resonance assignments and secondary structure of Bacillus subtil
Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Related Articles Polypeptide backbone resonance assignments and secondary structure of Bacillus subtilis enzyme IIIglc determined by two-dimensional and three-dimensional heteronuclear NMR spectroscopy.
Biochemistry. 1991 Jul 16;30(28):6896-907
Authors: Fairbrother WJ, Cavanagh J, Dyson HJ, Palmer AG, Sutrina SL, Reizer J, Saier MH, Wright PE
The enzyme...
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[NMR paper] Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double
Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Related Articles Assignment of the side-chain 1H and 13C resonances of interleukin-1 beta using double- and triple-resonance heteronuclear three-dimensional NMR spectroscopy.
Biochemistry. 1990 Sep 4;29(35):8172-84
Authors: Clore GM, Bax A, Driscoll PC, Wingfield PT, Gronenborn AM
The assignment of the aliphatic 1H and 13C resonances of IL-1 beta, a protein of 153 residues and molecular...
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[NMR paper] Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse
Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Related Articles Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy.
Biochemistry. 1990 Aug 14;29(32):7387-401
Authors: Clore GM, Driscoll PC, Wingfield PT, Gronenborn AM
The backbone dynamics of uniformly 15N-labeled interleukin-1 beta are investigated by using two-dimensional inverse detected heteronuclear 15N-1H NMR...
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[NMR paper] Determination of the secondary structure and molecular topology of interleukin-1 beta
Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy.
Related Articles Determination of the secondary structure and molecular topology of interleukin-1 beta by use of two- and three-dimensional heteronuclear 15N-1H NMR spectroscopy.
Biochemistry. 1990 May 15;29(19):4668-82
Authors: Driscoll PC, Gronenborn AM, Wingfield PT, Clore GM
A study of the regular secondary structure elements of recombinant human interleukin-1 beta has been...
Complete resonance assignment for the polypeptide backbone of interleukin 1 beta usin
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