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Blaine H. Mooers, Ph.D.

Affiliations: 
Biochemistry and Mol Biol University of Oklahoma Health Sciences Center, Oklahoma City, OK, United States 
Area:
RNA structure, crystallography
Website:
http://www.oumedicine.com/department-of-biochemistry-and-molecular-biology/faculty/blaine-mooers-ph-d-
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"Blaine Mooers"
Mean distance: 8.66
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Cross-listing: Crystallography Tree

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Parents

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P. Shing Ho grad student 1992-1997 Oregon State
Brian W. Matthews post-doc 1997-2006 University of Oregon

Children

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Collaborators

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John E. Hearst collaborator 1994-1997 Oregon State
Stephen L. Mayo collaborator 1999-2003 University of Oregon
John Andrew Berglund collaborator 2003-2005 University of Oregon
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Publications

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Mooers B, Gulati S, Kumar V, et al. (2017) Atomic structures of kinetoplastid RNA editing sites Acta Crystallographica Section A. 73
Gu X, Mooers BH, Thomas LM, et al. (2015) Structures and Energetics of Four Adjacent G·U Pairs That Stabilize an RNA Helix. The Journal of Physical Chemistry. B. 119: 13252-61
Mooers BH, Baase WA, Wray JW, et al. (2009) Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. Protein Science : a Publication of the Protein Society. 18: 871-80
Mooers BH, Tronrud DE, Matthews BW. (2009) Evaluation at atomic resolution of the role of strain in destabilizing the temperature-sensitive T4 lysozyme mutant Arg 96 --> His. Protein Science : a Publication of the Protein Society. 18: 863-70
Mooers BH, Matthews BW. (2006) Extension to 2268 atoms of direct methods in the ab initio determination of the unknown structure of bacteriophage P22 lysozyme. Acta Crystallographica. Section D, Biological Crystallography. 62: 165-76
Mooers BH, Logue JS, Berglund JA. (2005) The structural basis of myotonic dystrophy from the crystal structure of CUG repeats. Proceedings of the National Academy of Sciences of the United States of America. 102: 16626-31
Mooers BH, Matthews BW. (2004) Use of an ion-binding site to bypass the 1000-atom limit to structure determination by direct methods. Acta Crystallographica. Section D, Biological Crystallography. 60: 1726-37
Sagermann M, Baase WA, Mooers BH, et al. (2004) Relocation or duplication of the helix A sequence of T4 lysozyme causes only modest changes in structure but can increase or decrease the rate of folding. Biochemistry. 43: 1296-301
Mooers BH, Datta D, Baase WA, et al. (2003) Repacking the Core of T4 lysozyme by automated design. Journal of Molecular Biology. 332: 741-56
Gassner NC, Baase WA, Mooers BH, et al. (2003) Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability. Biophysical Chemistry. 100: 325-40
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