✦ LIBER ✦

1-13C amino acid selective labeling in a2H15N background for NMR studies of large proteins

✍ Scribed by Koh Takeuchi; Elise Ng; Thomas J. Malia; Gerhard Wagner

Publisher: Springer Netherlands
Year: 2007
Tongue: English
Weight: 569 KB
Volume: 38
Category: Article
ISSN: 0925-2738
DOI: 10.1007/s10858-007-9152-z

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Carbonyl carbon label selective (CCLS)1H

Carbonyl carbon label selective (CCLS)1H–15N HSQC experiment for improved detection of backbone13C–15N cross peaks in larger proteins

✍ Marco Tonelli; Larry R. Masterson; Klaas Hallenga; Gianluigi Veglia; John L. Mar 📂 Article 📅 2007 🏛 Springer Netherlands 🌐 English ⚖ 441 KB

HCN, A Triple-Resonance NMR Technique fo

HCN, A Triple-Resonance NMR Technique for Selective Observation of Histidine and Tryptophan Side Chains in13C/15N-Labeled Proteins

✍ James L. Sudmeier; Elissa L. Ash; Ulrich L. Günther; Xuelian Luo; Peter A. Bullo 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 299 KB

HCN, a new 3D NMR technique for stepwise coherence transfer rarely sufficient to establish the mechanism through which from 1 H to 13 C to 15 N and reverse through direct spin couplings it participates in the protein's function. The structure may 1 J CH and 1 J CN , is presented as a method for dete

13C CP MAS and high-resolution 1H, 13C,

13C CP MAS and high-resolution 1H, 13C, 15N NMR study of new ureido sugars, derivatives of 2-amino-2-deoxy-β-d-glucopyranose and l-amino acid

✍ Iwona Wawer; Boguslawa Piekarska-Bartoszewicz; Andrzej Temeriusz 📂 Article 📅 1995 🏛 Elsevier Science 🌐 English ⚖ 578 KB

Ureido sugars with seven various L-amino acid ester residues were studied by means of 'H, "C, and "N NMR in solution and 13C CP MAS in the solid state. The chemical shifts and coupling constants in the 'H, t3C, and "N NMR spectra indicated that the replacement of one amino acid residue by another ha

A JCH-Modulated 2D (HACACO)NH Pulse Sche

A JCH-Modulated 2D (HACACO)NH Pulse Scheme for Quantitative Measurement of 13Cα–1Hα Couplings in 15N, 13C-Labeled Proteins

✍ T.Kevin Hitchens; Scott A. McCallum; Gordon S. Rule 📂 Article 📅 1999 🏛 Elsevier Science 🌐 English ⚖ 73 KB

A triple-resonance pulse sequence is presented for the quantitative measurement of 1 H ␣ -13 C ␣ single-bond couplings in 15 N, 13 C uniformly labeled proteins. This 1 J CH -modulated (HACACO)NH experiment yields 1 H N -15 N-correlated 2D spectra in which the amplitude of each peak is modulated by t

The 2D NMR Experiments H(C)CO2and HCCO2f

The 2D NMR Experiments H(C)CO2and HCCO2for Assignment and pH Titration of Carboxylate Groups in Uniformly15N/13C-Labeled Proteins

✍ Maurizio Pellecchia; Hideo Iwai; Thomas Szyperski; Kurt Wüthrich 📂 Article 📅 1997 🏛 Elsevier Science 🌐 English ⚖ 112 KB

A 3D NOESY-(HCACO)NH experiment for the

A 3D NOESY-(HCACO)NH experiment for the measurement of NOEs involving1Hαin13C-/15N-labeled proteins dissolved in H2O

✍ Weixing Zhang; William H. Gmeiner 📂 Article 📅 1996 🏛 Springer Netherlands 🌐 English ⚖ 223 KB

A 3D NOESY-(HCACO)NH experiment is described that transfers NOEs from 1H alpha to the backbone 1Hn in the succeeding residue for detection. Using this strategy, NOEs involving 1H alpha protons that resonate exactly at the water frequency can be detected. NOEs from an overlapping 1H alpha proton that