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Chemical shift dispersion and secondary structure prediction in unfolded and partly folded proteins
Author(s) -
Yao Jian,
Dyson H.Jane,
Wright Peter E
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01474-9
Subject(s) - dispersion (optics) , chemistry , chemical shift , alpha (finance) , beta (programming language) , protein secondary structure , crystallography , resonance (particle physics) , heteronuclear single quantum coherence spectroscopy , protein structure , chemical physics , nuclear magnetic resonance , nuclear magnetic resonance spectroscopy , biochemistry , physics , stereochemistry , atomic physics , optics , medicine , construct validity , nursing , computer science , patient satisfaction , programming language
The intrinsic chemical shift dispersion for 15 N, 1 HN, 13 C α , 1 H α , 13 C β and 13 CO 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 13 C α , 1 H α , and 13 C β resonances for the unfolded proteins is poor, whereas the dispersion of 15 N, 1 HN and 13 CO 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 13 C α , 1 H α , and 13 C 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 15 N, 1 HN and, in particular, the 13 CO nuclei, are indicated for use with unfolded or partially folded proteins.