An improved technique for correlating backbone amide protons with 15N and Hα protons (HN(CA)H) in isotopically enriched proteins

[1]  A M Gronenborn,et al.  Four-dimensional heteronuclear triple-resonance NMR spectroscopy of interleukin-1 beta in solution. , 1990, Science.

[2]  I. Campbell,et al.  Comparison of techniques for 1H-detected heteronuclear 1H15N Spectroscopy , 1990 .

[3]  A. Bax,et al.  Complete proton and carbon-13 assignments of coenzyme B12 through the use of new two-dimensional NMR experiments , 1986 .

[4]  Robert Powers,et al.  Three-dimensional triple-resonance NMR of 13C/15N-enriched proteins using constant-time evolution , 1991 .

[5]  B. Erni,et al.  The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA. , 1987, The Journal of biological chemistry.

[6]  L. Kay,et al.  Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins , 1990 .

[7]  B. Erni,et al.  Mannose permease of Escherichia coli. Domain structure and function of the phosphorylating subunit. , 1989, The Journal of biological chemistry.

[8]  Gareth A. Morris,et al.  Enhancement of nuclear magnetic resonance signals by polarization transfer , 1979 .

[9]  K. Wüthrich,et al.  Application of phase sensitive two-dimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. , 1983, Biochemical and biophysical research communications.

[10]  M Ikura,et al.  An efficient 3D NMR technique for correlating the proton and15N backbone amide resonances with the α-carbon of the preceding residue in uniformly15N/13C enriched proteins , 1991, Journal of biomolecular NMR.

[11]  Four-dimensional heteronuclear triple-resonance NMR of isotopically enriched proteins for sequential assignment of backbone atoms , 1991 .

[12]  L. Kay,et al.  A novel approach for sequential assignment of proton, carbon-13, and nitrogen-15 spectra of larger proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin , 1990 .

[13]  L. Kay,et al.  A novel approach for sequential assignment of 1H, 13C, and 15N spectra of proteins: heteronuclear triple-resonance three-dimensional NMR spectroscopy. Application to calmodulin. , 1990, Biochemistry.

[14]  Paul C. Driscoll,et al.  Practical aspects of proton-carbon-carbon-proton three-dimensional correlation spectroscopy of 13C-labeled proteins , 1990 .

[15]  G. Wagner,et al.  A new 3D HN(CA)HA experiment for obtaining fingerprint HN-Hα cross peaks in15N- and13C-labeled proteins , 1992 .

[16]  S. Grzesiek,et al.  Improved 3D triple-resonance NMR techniques applied to a 31 kDa protein , 1992 .

[17]  G. Marius Clore,et al.  Applications of three- and four-dimensional heteronuclear NMR spectroscopy to protein structure determination , 1991 .

[18]  G. Bodenhausen,et al.  Multiple quantum spin-echo spectroscopy , 1980 .

[19]  L. Kay,et al.  The design and optimization of complex NMR experiments. Application to a triple-resonance pulse scheme correlating Hα, NH, and 15N chemical shifts in 15N13C-labeled proteins , 1991 .

[20]  L. Mueller,et al.  Observation of labile amide protons via indirect detection of 15N single-quantum transitions , 1991 .