13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues

Author:

Shu Irene,Scian Michele,Stewart James M.,Kier Brandon L.,Andersen Niels H.

Publisher

Springer Science and Business Media LLC

Subject

Spectroscopy,Biochemistry

Reference51 articles.

1. Andersen NH, Cort JR, Liu ZH, Sjoberg SJ, Tong H (1996) Cold denaturation of monomeric peptide helices. J Am Chem Soc 118:10309–10310

2. Andersen NH, Neidigh JW, Harris SM, Lee GM, Liu ZH, Tong H (1997) Extracting information from the temperature gradients of polypeptide NH chemical shifts. 1. The importance of conformational averaging. J Am Chem Soc 119:8547–8561

3. Andersen NH, Dyer RB, Fesinmeyer RM, Gai F, Liu ZH, Neidigh JW, Tong H (1999) Effect of hexafluoroisopropanol on the thermodynamics of peptide secondary structure formation. J Am Chem Soc 121:9879–9880

4. Andersen NH, Barua B, Fesinmeyer RM, Hudson FM, Lin JC, Euser A, White GW (2002) Chemical shifts, the ultimate test of peptide folding cooperativity. In: Benedetti E, Pedone C (eds) Proceedings of the 27th European peptide symposium, pp 824–825

5. Andersen NH, Fesinmeyer RM, Hudson FM (2004) Analysis of peptide β-sheet models using chemical shift deviations. In: Chorev M, Sawyer KT (eds) Peptide revolution: genetics, proteomics & therapeutics. Proceedings of the 18th American peptide symposium, pp 462–463

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