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Proceedings of the National Academy of Sciences of the United States of America|May 26, 1999
Structural characterization of an engineered tandem repeat contrasts the importance of context and sequence in protein foldingM Sagermann, W A Baase, B W MatthewsScience (New York, N.Y.)|June 11, 1993
Structural basis of amino acid alpha helix propensityM Blaber, X J Zhang, B W MatthewsProceedings of the National Academy of Sciences of the United States of America|October 1, 1987
Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfoldingB W Matthews, H Nicholson, W J BecktelJournal of Molecular Biology|June 5, 1989
Crystallization and preliminary X-ray studies of Escherichia coli glycerol kinaseH R Faber, D W Pettigrew, S J RemingtonScience (New York, N.Y.)|January 30, 1987
Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bondD E Tronrud, H M Holden, B W MatthewsThe Journal of Biological Chemistry|February 5, 1992
Tolerance of T4 lysozyme to proline substitutions within the long interdomain alpha-helix illustrates the adaptability of proteins to potentially destabilizing lesionsU H Sauer, D P San, B W MatthewsMatrix (Stuttgart, Germany). Supplement|January 1, 1992
Structural basis for the action of thermolysinD E Tronrud, S L Roderick, B W MatthewsProtein Science : a Publication of the Protein Society|June 8, 2011
The role of calcium ions in the stability and instability of a thermolysin-like proteaseV G H Eijsink, B W Matthews, G VriendJournal of Molecular Biology|July 21, 1995
Protein flexibility and adaptability seen in 25 crystal forms of T4 lysozymeX J Zhang, J A Wozniak, B W MatthewsBiochemistry|January 4, 1983
Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitorM A Holmes, D E Tronrud, B W MatthewsPageof 19