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NH–NH Vector Correlation in Peptides by Solid-State NMR

✍ Scribed by B. Reif; M. Hohwy; C.P. Jaroniec; C.M. Rienstra; R.G. Griffin

Publisher
Elsevier Science
Year
2000
Tongue
English
Weight
309 KB
Volume
145
Category
Article
ISSN
1090-7807

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✦ Synopsis

We present a novel solid-state magic angle-spinning NMR method for measuring the NH i -NH i؉1 projection angle i,i؉1 in peptides. The experiment is applicable to uniformly 15 N-labeled peptides and is demonstrated on the chemotactic tripeptide N-formyl-L-Met-L-Leu-L-Phe. The projection angle i,i؉1 is directly related to the peptide backbone torsion angles i and i . The method utilizes the T-MREV recoupling scheme to restore 15 N-1 H interactions, and proton-mediated spin diffusion to establish 15 N-15 N correlations. T-MREV has recently been shown to increase the dynamic range of the 15 N-1 H recoupling by ␥-encoding, and permits an accurate determination of the recoupled NH dipolar interaction. The results are interpreted in a quasi-analytical fashion that permits efficient extraction of the structural parameters.

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