Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins

FEBS Letters

Dyson, H.Jane¹  Wright, Peter E¹  Yao, Jian¹ 

[1] Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA

关键词: NMR;    Residual structure;    Conformational preference;   

DOI  :  10.1016/S0014-5793(97)01474-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The intrinsic chemical shift dispersion for ¹⁵N, ¹HN, ¹³C^α, ¹H^α, ¹³C^β and ¹³CO resonances has been evaluated utilizing complete resonance assignment data for unfolded apomyoglobin, together with two other unfolded and five folded proteins, obtained from the literature. The dispersion of ¹³C^α, ¹H^α, and ¹³C^β resonances for the unfolded proteins is poor, whereas the dispersion of ¹⁵N, ¹HN and ¹³CO is much greater, reflecting the sensitivity of these nuclei to the nature of the neighboring amino acid in the primary sequence. By contrast, the dispersion of the ¹³C^α, ¹H^α, and ¹³C^β nuclei are much greater in the folded proteins, reflecting the well-known dependence of the environments of these nuclei on secondary and tertiary structure. These differences in chemical shift dispersion dictate differences in strategies for resonance assignment in unfolded proteins compared with those most commonly used for folded proteins. Strategies utilizing the superior chemical shift dispersion of the ¹⁵N, ¹HN and, in particular, the ¹³CO nuclei, are indicated for use with unfolded or partially folded proteins.

【 授权许可】

Unknown