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Literature DB >> 30465113

BEST and SOFAST experiments for resonance assignment of histidine and tyrosine side chains in ¹³C/¹⁵N labeled proteins.

Nina Eleni Christou¹, Bernhard Brutscher².

Abstract

Aromatic amino-acid side chains are essential components for the structure and function of proteins. We present herein a set of NMR experiments for time-efficient resonance assignment of histidine and tyrosine side chains in uniformly 13C/15N-labeled proteins. The use of band-selective 13C pulses allows to deal with linear chains of coupled spins, thus avoiding signal loss that occurs in branched spin systems during coherence transfer. Furthermore, our pulse schemes make use of longitudinal 1H relaxation enhancement, Ernst-angle excitation, and simultaneous detection of 1H and 13C steady-state polarization to achieve significant signal enhancements.

Entities: Chemical

Keywords: Aromatics; BEST; Histidine tautomerization; Longitudinal relaxation enhancement; NMR assignment

Mesh：

Substances：

Year: 2018 PMID： 30465113 DOI： 10.1007/s10858-018-0216-z

Source DB: PubMed Journal: J Biomol NMR ISSN： 0925-2738 Impact factor: 2.835

26 in total

1. Analysis of catalytic residues in enzyme active sites.

Authors: Gail J Bartlett; Craig T Porter; Neera Borkakoti; Janet M Thornton
Journal: J Mol Biol Date: 2002-11-15 Impact factor: 5.469

2. Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.

Authors: Jun Hu; Riqiang Fu; Katsuyuki Nishimura; Li Zhang; Huan-Xiang Zhou; David D Busath; Viksita Vijayvergiya; Timothy A Cross
Journal: Proc Natl Acad Sci U S A Date: 2006-04-21 Impact factor: 11.205

3. Biosynthetically directed fractional 13C labeling facilitates identification of Phe and Tyr aromatic signals in proteins.

Authors: Jaison Jacob; John M Louis; Issa Nesheiwat; Dennis A Torchia
Journal: J Biomol NMR Date: 2002-11 Impact factor: 2.835

4. Speeding up three-dimensional protein NMR experiments to a few minutes.

Authors: Paul Schanda; Hélène Van Melckebeke; Bernhard Brutscher
Journal: J Am Chem Soc Date: 2006-07-19 Impact factor: 15.419

5. Probing structure and functional dynamics of (large) proteins with aromatic rings: L-GFT-TROSY (4,3)D HCCH NMR spectroscopy.

Authors: Alexander Eletsky; Hanudatta S Atreya; Gaohua Liu; Thomas Szyperski
Journal: J Am Chem Soc Date: 2005-10-26 Impact factor: 15.419

6. Tautomerism of histidine 64 associated with proton transfer in catalysis of carbonic anhydrase.

Authors: Hideto Shimahara; Takuya Yoshida; Yasutaka Shibata; Masato Shimizu; Yoshimasa Kyogoku; Fumio Sakiyama; Takashi Nakazawa; Shin-ichi Tate; Shin-ya Ohki; Takeshi Kato; Hozumi Moriyama; Ken-ichi Kishida; Yasuo Tano; Tadayasu Ohkubo; Yuji Kobayashi
Journal: J Biol Chem Date: 2007-01-03 Impact factor: 5.157

7. SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds.

Authors: Paul Schanda; Eriks Kupce; Bernhard Brutscher
Journal: J Biomol NMR Date: 2005-12 Impact factor: 2.835

8. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.

Authors: Paul Schanda; Bernhard Brutscher
Journal: J Am Chem Soc Date: 2005-06-08 Impact factor: 15.419

BEST and SOFAST experiments for resonance assignment of histidine and tyrosine side chains in ¹³C/¹⁵N labeled proteins.

1. Analysis of catalytic residues in enzyme active sites.

2. Histidines, heart of the hydrogen ion channel from influenza A virus: toward an understanding of conductance and proton selectivity.

3. Biosynthetically directed fractional 13C labeling facilitates identification of Phe and Tyr aromatic signals in proteins.

4. Speeding up three-dimensional protein NMR experiments to a few minutes.

5. Probing structure and functional dynamics of (large) proteins with aromatic rings: L-GFT-TROSY (4,3)D HCCH NMR spectroscopy.

6. Tautomerism of histidine 64 associated with proton transfer in catalysis of carbonic anhydrase.

7. SOFAST-HMQC experiments for recording two-dimensional heteronuclear correlation spectra of proteins within a few seconds.

8. Very fast two-dimensional NMR spectroscopy for real-time investigation of dynamic events in proteins on the time scale of seconds.

9. Identification of histidine tautomers in proteins by 2D 1H/13C(delta2) one-bond correlated NMR.

10. Longitudinal (1)H relaxation optimization in TROSY NMR spectroscopy.

1. NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein.

2. Visualizing protein breathing motions associated with aromatic ring flipping.