Structural determinants of functional behavior in distal pocket mutants of myoglobin

Autor: Quillin, Michael L.

The physiological role of myoglobin depends on the modulation of heme activity by the protein. The hypothesis that functional properties are governed by conserved residues in the distal pocket has been tested by site-directed mutagenesis of three res

Externí odkaz: http://hdl.handle.net/1911/16871

Determination of Solvent Content in Cavities in IL-1β Using Experimentally Phased Electron Density

Autor: Quillin, Michael L., Wingfield, Paul T., Matthews, Brian W.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America, 2006 Dec . 103(52), 19749-19753.

Externí odkaz: https://www.jstor.org/stable/30051382

Selling candles in a post-Edison world: phasing with noble gases bound within engineered sites.

Autor: Quillin, Michael L.¹, Matthews, Brian W.¹ brian@uoxray.uoregon.edu

Publikováno v: Acta Crystallographica: Section D (Wiley-Blackwell). Nov2003, Vol. 59 Issue 11, p1930-1934. 5p.

Use of experimental crystallographic phases to examine the hydration of polar and nonpolar cavities in T4 lysozyme.

Autor: Lijun Liu, Quillin, Michael L., Matthews, Brian W.

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America; 9/23/2008, Vol. 105 Issue 38, p14406-14411, 6p, 1 Black and White Photograph, 4 Charts

Identification of an SH3-Binding Motif in a New Class of Methionine Aminopeptidases from Mycobacterium tuberculosis Suggests a Mode of Interaction with the Ribosome.

Autor: Addlagatta, Anthony, Quillin, Michael L., Omotoso, Omonike, Liu, Jun O., Matthews, Brian W.

Publikováno v: Biochemistry; 5/17/2005, Vol. 44 Issue 19, p7166-7174, 9p