𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Determination of Chemical Shift Anisotropy Tensors of Carbonyl Nuclei in Proteins through Cross-Correlated Relaxation in NMR

✍ Scribed by Federico Cisnetti; Karine Loth; Philippe Pelupessy; Geoffrey Bodenhausen

Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
225 KB
Volume
5
Category
Article
ISSN
1439-4235

No coin nor oath required. For personal study only.

✦ Synopsis

Abstract

The principal components and orientations of the chemical shift anisotropy (CSA) tensors of nearly all ^13^C carbonyl nuclei in a small protein have been determined in isotropic solution by a combination of three complementary cross‐correlation measurements.

📜 SIMILAR VOLUMES

Measurement of Cross Correlation between
Measurement of Cross Correlation between Dipolar Coupling and Chemical Shift Anisotropy in the Spin Relaxation of13C,15N-Labeled Proteins
✍ Ranajeet Ghose; Kai Huang; James H Prestegard 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 259 KB

We present a simple method for extracting interference effects between chemical shift anisotropy (CSA) and dipolar coupling from spin relaxation measurements in macromolecules, and we apply this method to extracting cross-correlation rates involving interference of amide 15N CSA and 15N-1H dipolar c

Determination of the Peptide Torsion Ang
Determination of the Peptide Torsion Angle φ by15N Chemical Shift and13Cα-1HαDipolar Tensor Correlation in Solid-State MAS NMR
✍ M. Hong; J.D. Gross; W. Hu; R.G. Griffin 📂 Article 📅 1998 🏛 Elsevier Science 🌐 English ⚖ 214 KB

We demonstrate a dipolar-chemical shift correlation technique for sign-sensitive determination of the torsion angle in solid peptides and proteins under magic-angle spinning. The indirect dimension of the experiment is obtained by separate but synchronous evolution of the magnetization under the 15