The nature of trypsin-pancreatic trypsin inhibitor binding: free energy calculation of Tyr39→ Phe39 mutation in trypsin
Author:
Publisher
Wiley
Subject
Endocrinology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1997.tb01198.x/fullpdf
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1. The geometry of the reactive site and of the peptide groups in trypsin, trypsinogen and its complexes with inhibitors
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1. Free Energy Calculations: Use and Limitations in Predicting Ligand Binding Affinities;Reviews in Computational Chemistry;2007-01-05
2. Parametrization of Synthetic Amino Acids;The Journal of Physical Chemistry B;2003-11-27
3. Theoretical study of the amino acid interactions in the binding region of the trypsin–pancreatic trypsin inhibitor complex;Journal of Molecular Structure: THEOCHEM;2002-03
4. MODELLING ENZYME - LIGAND INTERACTIONS;Theoretical and Computational Chemistry;2001
5. Reply;Gastroenterology;2000-07
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