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Free energy calculations show that acidic P1 variants undergo large pKa shifts upon binding to trypsin.
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology.
2006 (English)In: Proteins, ISSN 1097-0134, Vol. 64, no 3, p. 740-8Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2006. Vol. 64, no 3, p. 740-8
Keywords [en]
Aprotinin/*chemistry/metabolism, Aspartic Acid/chemistry, Binding Sites, Computer Simulation, Crystallography; X-Ray, Entropy, Glutamic Acid/chemistry, Models; Molecular, Molecular Structure, Protein Binding, Protein Structure; Secondary, Protein Structure; Tertiary, Serine Endopeptidases/chemistry/metabolism, Structure-Activity Relationship, Substrate Specificity, Thermodynamics, Trypsin/*chemistry/metabolism, Trypsin Inhibitors/chemistry/metabolism
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URN: urn:nbn:se:uu:diva-20998PubMedID: 16752417OAI: oai:DiVA.org:uu-20998DiVA, id: diva2:48771
Available from: 2008-06-05 Created: 2008-06-05 Last updated: 2011-01-11

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Åqvist, Johan

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