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Determination of peptide φ angles in solids by relayed anisotropy correlation NMR

✍ Scribed by Yoshitaka Ishii; Koichi Hirao; Takehiko Terao; Tsutomu Terauchi; Makoto Oba; Kozaburo Nishiyama; Masatsune Kainosho

Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
255 KB
Volume
11
Category
Article
ISSN
0926-2040

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✦ Synopsis

A solid state NMR method is presented for determination of a backbone dihedral angle phi in peptides, being based on the previously reported method, relayed anisotropy correlation (RACO) NMR [Y. Ishii et al., Chem. Phys. Lett. 256 (1996) 133]. In the present method, the 15N-1H and the 13C-1H dipolar tensors in the 1H-15N-13C-1H system are two-dimensionally (2D) correlated via polarization transfer from 15N to 13C under magic angle spinning (MAS). This method was applied to N-acetyl[1,2-13C,15N]D,L-valine, and the H-C-N-H dihedral angle was determined to be 154.0 +/- 1.4 degrees or 206.0 +/- 1.4 degrees, the former agreeing with the X-ray value of 154 +/- 5 degrees.

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## Abstract The ϕ angle in a cyclic peptide is determined by the combined use of homonuclear and heteronuclear coupling constants. Two of the four coupling constants that define the ϕ angle in a peptide are determined exactly, two qualitatively. Via Karplus‐type equations, they are transformed into