Thermodynamics of Binding of 2-Methoxy-3-isopropylpyrazine and 2-Methoxy-3-isobutylpyrazine to the Major Urinary Protein

In the present study we examine the thermodynamics of binding of two related pyrazine-derived ligands to the major urinary protein, MUP-I, using a combination of isothermal titration calorimetry (ITC), X-ray crystallography, and NMR backbone 15N and methyl side-chain 2H relaxation measurements. Glob...

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Veröffentlicht in:	Journal of the American Chemical Society 2004-02, Vol.126 (6), p.1675-1681
Hauptverfasser:	Bingham, Richard J., Findlay, John B. C., Hsieh, Shih-Yang, Kalverda, Arnout P., Kjellberg, Alexandra, Perazzolo, Chiara, Phillips, Simon E. V., Seshadri, Kothandaraman, Trinh, Chi H., Turnbull, W. Bruce, Bodenhausen, Geoffrey, Homans, Steve W.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Biological and medical sciences Calorimetry Crystallography, X-Ray Fundamental and applied biological sciences. Psychology Interactions. Associations Intermolecular phenomena Molecular biophysics Molecular Sequence Data Nitrogen Isotopes Nuclear Magnetic Resonance, Biomolecular - methods Protein Binding Protein Conformation Proteins - chemistry Proteins - metabolism Pyrazines - chemistry Pyrazines - metabolism Thermodynamics
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