J Mol Biol. 1982 Sep 15;160(2):343-61.

Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance.

Wagner G, Wüthrich K.

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Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor. [Eur J Biochem. 1984]
Amide-proton exchange studies by two-dimensional correlated 1H NMR in two chemically modified analogs of the basic pancreatic trypsin inhibitor.
Wagner G, Stassinopoulou CI, Wüthrich K. Eur J Biochem. 1984 Dec 3; 145(2):431-6.
Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution. [Eur J Biochem. 1985]
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Amide proton exchange in proteins by EX1 kinetics: studies of the basic pancreatic trypsin inhibitor at variable p2H and temperature. [Biochemistry. 1985]
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Review Nuclear magnetic resonance studies of internal mobility in globular proteins. [Biochem Soc Symp. 1981]
Review Nuclear magnetic resonance studies of internal mobility in globular proteins.
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Review Two-dimensional NMR spectroscopy: an application to the study of flexibility of protein molecules. [Adv Biophys. 1981]
Review Two-dimensional NMR spectroscopy: an application to the study of flexibility of protein molecules.
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Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance.
J Mol Biol. 1982 Sep 15 ;160(2):343-61.

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Amide protein exchange and surface conformation of the basic pancreatic trypsin inhibitor in solution. Studies with two-dimensional nuclear magnetic resonance.

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