Conformational analysis by quantitative NOE measurements of the β-proton pairs across individual disulfide bonds in proteins
Author:
Publisher
Springer Science and Business Media LLC
Subject
Spectroscopy,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s10858-011-9587-0.pdf
Reference56 articles.
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4. Berndt KD, Güntert P, Orbons LP, Wüthrich K (1992) Determination of a high-quality nuclear magnetic resonance solution structure of the bovine pancreatic trypsin inhibitor and comparison with three crystal structures. J Mol Biol 277:757–775
5. Billeter M, Braun W, Wüthrich K (1982) Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton–proton distances and statistical analysis of proton–proton distances in single crystal protein conformations. J Mol Biol 155:321–346
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