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Local helix content in an alanine-rich peptide as determined by the complete set of 3JHNα coupling constants (1996)

Millhauser, Glenn L. ; Stenland, Chris J. ; Bolin, Kimberly A. ; [et al.]

Springer

Journal of biomolecular NMR 7 (1996), S. 331-334

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ISSN: 1573-5001

Keywords: J coupling ; Coupling constants ; Inverse fitting ; Alanine ; Helix ; Peptide

Source: Springer Online Journal Archives 1860-2000

Topics: Biology , Chemistry and Pharmacology

Notes: Summary Alanine-rich peptides serve as models for exploring the factors that control helix structure in peptides and proteins. Scalar CαH-NH couplings (3JHNα) are an extremely useful measure of local helix content; however, the large alanine content in these peptides leads to significant signal overlap in the CαH region of 1H 2D NMR spectra. Quantitative determination of all possible 3JHNα values is, therefore, very challenging. Szyperski and co-workers [(1992) J. Magn. Reson., 99, 552–560] have recently developed a method for determining 3JHNα from NOESY spectra. Because 3JHNα may be determined from 2D peaks outside of the CαH region, there is a much greater likelihood of identifying resolved resonances and measuring the associated coupling constants. It is demonstrated here that 3JHNα can be obtained for every residue in the helical peptide Ac-(AAAAK)3A-NH2. The resulting 3JHNα profile clearly identifies a helical structure in the middle of the peptide and further suggests that the respective helix termini unfold via distinct pathways.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00200434

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Synthesis and conformational studies of peptides containing TOAC, a spin-labelled Cα,α-disubstituted glycine (1995)

Toniolo, Claudio ; Valente, Ezio ; Formaggio, Fernando ; [et al.]

New York, NY [u.a.] : Wiley-Blackwell

Journal of Peptide Science 1 (1995), S. 45-57

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ISSN: 1075-2617

Keywords: β-bend ; 310-helix ; peptide conformational analysis ; spin-labelled amino acid ; TOAC peptides ; Chemistry ; Biochemistry and Biotechnology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: A variety of host L-alanine homo-peptides (to the pentamer) containing one or two spin-labelled TOAC (2,2,6,6-tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid) residues were synthesized by solution methods and fully characterized. The conformational features of the terminally blocked, doubly spin-labelled-TOAC-(Ala)2-TOAC-Ala- pentapeptide were examined in the crystal state by X-ray diffraction and in solution using a combination of techniques (Fourier transform infrared, circular dichroism, cyclic voltammetry and electron spin resonance) in comparison with singly labelled shorter peptides. The 310-helical structure of the pentapeptide, promoted by the two Cα,α-disubstituted glycines under favourable experimental conditions, allows an interaction to take place between the two nitroxide TOAC side chains spaced by one turn of the helix. Taken together, these results suggest that TOAC is an excellent probe for exploring bends and helices in doubly labelled peptides.

Additional Material: 8 Ill.