'Random coil' 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG.


:Proton chemical shifts of a series of disordered linear peptides (H-Gly-Gly-X-Gly-Gly-OH, with X being one of the 20 naturally occurring amino acids) have been obtained using 1D and 2D 1H NMR at pH 5.0 as a function of temperature and solvent composition. The use of 2D methods has allowed some ambiguities in side-chain assignments in previous studies to be resolved. An additional benefit of the temperature data is that they can be used to obtain 'random coil' amide proton chemical shifts at any temperature between 278 and 318 K by interpolation. Changes of chemical shift as a function of trifluoroethanol concentration have also been determined at a variety of temperatures for a subset of peptides. Significant changes are found in backbone and side-chain amide proton chemical shifts in these 'random coil' peptides with increasing amounts of trifluoroethanol, suggesting that caution is required when interpreting chemical shift changes as a measure of helix formation in peptides in the presence of this solvent. Comparison of the proton chemical shifts obtained here for H-Gly-Gly-X-Gly-Gly-OH with those for H-Gly-Gly-X-Ala-OH [Bundi, A. and Wüthrich, K., (1979) Biopolymers, 18, 285-297] and for Ac-Gly-Gly-X-Ala-Gly-Gly-NH2 [Wishart, D.S., Bigam, C.G., Holm, A., Hodges, R.S. and Sykes, B.D. (1995) J. Biomol. NMR, 5, 67-81] generally shows good agreement for CH protons, but reveals significant variability for NH protons. Amide proton chemical shifts appear to be highly sensitive to local sequence variations and probably also to solution conditions. Caution must therefore be exercised in any structural interpretation based on amide proton chemical shifts.


J Biomol NMR


Merutka G,Dyson HJ,Wright PE




Has Abstract


1995-01-01 00:00:00












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    authors: Kloiber K,Schüler W,Konrat R

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    authors: Nabuurs SB,Krieger E,Spronk CA,Nederveen AJ,Vriend G,Vuister GW

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    authors: Lancelot N,Elbayed K,Piotto M

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  • Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.

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    authors: Antanasijevic A,Kingsley C,Basu A,Bowlin TL,Rong L,Caffrey M

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    authors: Giesen AW,Homans SW,Brown JM

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    authors: Sathyamoorthy B,Lee J,Kimsey I,Ganser LR,Al-Hashimi H

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    journal_title:Journal of biomolecular NMR

    pub_type: 杂志文章


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    authors: Yao S,Howlett GJ,Norton RS

    更新日期:2000-02-01 00:00:00