Related Articles1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Biochemistry. 1991 Oct 15;30(41):10043-57
Authors: Pelton JG, Torchia DA, Meadow ND, Wong CY, Roseman S
IIIGlc is an 18.1-kDa signal-transducing phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase system (PTS) of Escherichia coli. Virtually complete (98%) backbone 1H, 15N, and 13C nuclear magnetic resonance (NMR) signal assignments were determined by using a battery of triple-resonance three-dimensional (3D) NMR pulse sequences. In addition, nearly complete (1H, 95%; 13C, 85%) side-chain 1H and 13C signal assignments were obtained from an analysis of 3D 13C HCCH-COSY and HCCH-TOCSY spectra. These experiments rely almost exclusively upon one- and two-bond J couplings to transfer magnetization and to correlate proton and heteronuclear NMR signals. Hence, essentially complete signal assignments of this 168-residue protein were made without any assumptions regarding secondary structure and without the aid of a crystal structure, which is not yet available. Moreover, only three samples, one uniformly 15N-enriched, one uniformly 15N/13C-enriched, and one containing a few types of amino acids labeled with 15N and/or 13C, were needed to make the assignments. The backbone assignments together with the 3D 15N NOESY-HMQC and 13C NOESY-HMQC data have provided extensive information about the secondary structure of this protein [Pelton, J.G., Torchia, D.A., Meadow, N.D., Wong, C.-Y., & Roseman, S (1991) Proc. Natl. Acad. Sci. U.S.A. 88, 3479-3488]. The nearly complete set of backbone and side-chain atom assignments reported herein provide a basis for studies of the three-dimensional structure and dynamics of IIIGlc as well as its interactions with a variety of membrane and cytoplasmic proteins.
[NMR paper] Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by
Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy.
Biochemistry. 1996 May 21;35(20):6399-405
Authors: Jung H, Windhaber R, Palm D, Schnackerz KD
The peptide T345-359 representing the fourth intracellular loop of the avian...
nmrlearner
Journal club
0
08-22-2010 02:27 PM
[NMR paper] Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigatio
Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
Related Articles Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
J Magn Reson B. 1994 Jul;104(3):230-9
Authors: Bertini I, Jonsson BH, Luchinat C, Pierattelli R, Vila AJ
The title protein with MW 30,000 containing high-spin cobalt (II) has been...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigatio
Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
Related Articles Strategies of signal assignments in paramagnetic metalloproteins. An NMR investigation of the thiocyanate adduct of the cobalt (II)-substituted human carbonic anhydrase II.
J Magn Reson B. 1994 Jul;104(3):230-9
Authors: Bertini I, Jonsson BH, Luchinat C, Pierattelli R, Vila AJ
The title protein with MW 30,000 containing high-spin cobalt (II) has been...
nmrlearner
Journal club
0
08-22-2010 03:33 AM
[NMR paper] Transforming growth factor beta 1: NMR signal assignments of the recombinant protein
Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells.
Related Articles Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells.
Biochemistry. 1993 Feb 2;32(4):1152-63
Authors: Archer SJ, Bax A, Roberts AB, Sporn MB, Ogawa Y, Piez KA, Weatherbee JA, Tsang ML, Lucas R, Zheng BL
The transforming growth factor beta s are a homologous family of...
nmrlearner
Journal club
0
08-21-2010 11:53 PM
[NMR paper] Secondary structure of the phosphocarrier protein IIIGlc, a signal-transducing protei
Secondary structure of the phosphocarrier protein IIIGlc, a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Secondary structure of the phosphocarrier protein IIIGlc, a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy.
Proc Natl Acad Sci U S A. 1991 Apr 15;88(8):3479-83
Authors: Pelton JG,...
nmrlearner
Journal club
0
08-21-2010 11:16 PM
[NMR paper] 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Es
1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Related Articles 1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Escherichia coli, using three-dimensional triple-resonance techniques.
Biochemistry. 1991 Oct 15;30(41):10043-57
Authors: Pelton JG, Torchia DA, Meadow ND, Wong CY, Roseman S
IIIGlc is an 18.1-kDa signal-transducing phosphocarrier protein of the phosphoenolpyruvate:glycose phosphotransferase...
1H, 15N, and 13C NMR signal assignments of IIIGlc, a signal-transducing protein of Es
Linear Mode
