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Mike Harms

Mike Harms

Assistant Professor, Chemistry and Biochemistry
Member, IMB

Ph.D. Johns Hopkins University
B.S. Oregon State University

Email
Lab website
Office: Willamette Hall Room 340A
Office Phone: 541-346-9002
Lab: Willamette Hall Room 340
Lab Phone: 541-346-9003

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Research Interests

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RNA is an exceptionally versatile biological macromolecule, in turn acting as an information carrier, genome, catalyst, regulator of gene expression, structural scaffold, and much more. Furthermore, RNA provides a highly tunable scaffold that can be used to build sensors and nanostructures. My research will focus on the development and application of spectroscopic methods to address questions regarding RNA structure and dynamics. Crystal structures and cryo-electron microscopy have provided high-resolution snapshots of many different RNA species, and we seek to complement those studies by using novel optical spectroscopy methods to interrogate RNA under native conditions. We are particularly interested in RNAs whose biological functions depend directly on their abilities to fold into and interconvert between specific structures. Our initial studies will focus on riboswitches, which are bacterial sensor RNAs that regulate gene expression by re-folding upon binding of a ligand, and on the spliceosome, which catalyzes the reaction of pre-messenger RNA splicing, a key step in gene expression in eukaryotes. In the case of riboswitches, the structure of the folded RNA confers sensitivity to its ligand, and in the case of splicing, the structure of the pre-mRNA is one of many factors that determines the location at which splicing occurs and its efficiency.

Recent publications

(pulled from pubmed)

Recent publications

(pulled from pubmed)

Thermodynamic system drift in protein evolution.
Hart KM, Harms MJ, Schmidt BH, Elya C, Thornton JW, Marqusee S
PLoS Biol 2014 Nov;12(11):e1001994
Biophysical mechanisms for large-effect mutations in the evolution of steroid hormone receptors.
Harms MJ, Eick GN, Goswami D, Colucci JK, Griffin PR, Ortlund EA, Thornton JW
Proc Natl Acad Sci U S A 2013 Jul 9;110(28):11475-80
Evolution of minimal specificity and promiscuity in steroid hormone receptors.
Eick GN, Colucci JK, Harms MJ, Ortlund EA, Thornton JW
PLoS Genet 2012;8(11):e1003072
Arginine residues at internal positions in a protein are always charged.
Harms MJ, Schlessman JL, Sue GR, García-Moreno B
Proc Natl Acad Sci U S A 2011 Nov 22;108(47):18954-9
Analyzing protein structure and function using ancestral gene reconstruction.
Harms MJ, Thornton JW
Curr Opin Struct Biol 2010 Jun;20(3):360-6
Protein evolution by molecular tinkering: diversification of the nuclear receptor superfamily from a ligand-dependent ancestor.
Bridgham JT, Eick GN, Larroux C, Deshpande K, Harms MJ, Gauthier ME, Ortlund EA, Degnan BM, Thornton JW
PLoS Biol 2010 Oct 5;8(10)
The pK(a) values of acidic and basic residues buried at the same internal location in a protein are governed by different factors.
Harms MJ, Castañeda CA, Schlessman JL, Sue GR, Isom DG, Cannon BR, García-Moreno E B
J Mol Biol 2009 May 29;389(1):34-47
A buried lysine that titrates with a normal pKa: role of conformational flexibility at the protein-water interface as a determinant of pKa values.
Harms MJ, Schlessman JL, Chimenti MS, Sue GR, Damjanović A, García-Moreno B
Protein Sci 2008 May;17(5):833-45
Laser light-scattering evidence for an altered association of beta B1-crystallin deamidated in the connecting peptide.
Harms MJ, Wilmarth PA, Kapfer DM, Steel EA, David LL, Bächinger HP, Lampi KJ
Protein Sci 2004 Mar;13(3):678-86