Showing results (71-80 of 193) with videos related to
Sort By:
Pageof 20
Science (New York, N.Y.)|December 24, 1993
A covalent enzyme-substrate intermediate with saccharide distortion in a mutant T4 lysozymeR Kuroki, L H Weaver, B W MatthewsNature|August 4, 1988
Hydrophobic stabilization in T4 lysozyme determined directly by multiple substitutions of Ile 3M Matsumura, W J Becktel, B W MatthewsNature|December 15, 1988
Enhanced protein thermostability from designed mutations that interact with alpha-helix dipolesH Nicholson, W J Becktel, B W MatthewsProceedings 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 BecktelProteins|September 1, 1996
Crystallization and preliminary crystallographic analysis of tetrahydrodipicolinate-N-succinyltransferaseD A Binder, J S Blanchard, S L RoderickBiochemistry|July 22, 1998
The conformational change and active site structure of tetrahydrodipicolinate N-succinyltransferaseT W Beaman, J S Blanchard, S L RoderickThe 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 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 VriendPageof 20