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Literature DB >> 10527755

Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy.

Abstract

Two modifications to sensitivity-enhanced gradient-selected TROSY-based triple-resonance NMR experiments are proposed that reduce the overall duration of the pulse sequences and minimize radiation damping effects on water-flipback solvent suppression. The modifications are illustrated for the HNCO-TROSY experiment, but are applicable to all triple-resonance experiments that detect proton magnetization after a reverse polarization transfer step from a (15)N spin. The methods are applied to yeast triosephosphate isomerase, a symmetric dimer with 248 amino acid residues per monomer. Copyright 1999 Academic Press.

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Year: 1999 PMID： 10527755 DOI： 10.1006/jmre.1999.1891

Source DB: PubMed Journal: J Magn Reson ISSN： 1090-7807 Impact factor: 2.229

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Cited

47 in total

1. A new approach for obtaining sequential assignment of large proteins.

Authors: P Permi; A Annila
Journal: J Biomol NMR Date: 2001-06 Impact factor: 2.835

2. Non-uniformly sampled double-TROSY hNcaNH experiments for NMR sequential assignments of large proteins.

Authors: Dominique P Frueh; Zhen-Yu J Sun; David A Vosburg; Christopher T Walsh; Jeffrey C Hoch; Gerhard Wagner
Journal: J Am Chem Soc Date: 2006-05-03 Impact factor: 15.419

3. Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [(15)N,(1)H]-TROSY-HNC experiment.

Authors: Hans L J Wienk; Mitcheell M Martínez; Gary N Yalloway; Jürgen M Schmidt; Carlos Pérez; Heinz Rüterjans; Frank Löhr
Journal: J Biomol NMR Date: 2003-02 Impact factor: 2.835

4. A selective intra-HN(CA)CO experiment for the backbone assignment of deuterated proteins.

Authors: Daniel Nietlispach
Journal: J Biomol NMR Date: 2004-02 Impact factor: 2.835

5. The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.

Authors: Yongbo Zhang; Erik R P Zuiderweg
Journal: Proc Natl Acad Sci U S A Date: 2004-07-01 Impact factor: 11.205

6. Using codon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of human eIF2 alpha.

Authors: Takuhiro Ito; Gerhard Wagner
Journal: J Biomol NMR Date: 2004-04 Impact factor: 2.835

Transverse-relaxation-optimized (TROSY) gradient-enhanced triple-resonance NMR spectroscopy.

1. A new approach for obtaining sequential assignment of large proteins.

2. Non-uniformly sampled double-TROSY hNcaNH experiments for NMR sequential assignments of large proteins.

3. Simultaneous measurement of protein one-bond and two-bond nitrogen-carbon coupling constants using an internally referenced quantitative J-correlated [(15)N,(1)H]-TROSY-HNC experiment.

4. A selective intra-HN(CA)CO experiment for the backbone assignment of deuterated proteins.

5. The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.

6. Using codon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of human eIF2 alpha.

7. ¹H, ¹⁵N, and ¹³C backbone resonance assignments for the Yersinia protein tyrosine phosphatase YopH.

8. Intraresidual HNCA: an experiment for correlating only intraresidual backbone resonances.

9. Measurement of residual dipolar couplings from 1Halpha to 13Calpha and 15N using a simple HNCA-based experiment.

10. HNCO-based measurement of one-bond amide 15N-1H couplings with optimized precision.