Robert M. Fesinmeyer, Ph.D.

Affiliations: 
University of Washington, Seattle, Seattle, WA 
Area:
biorecognition
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"Robert Fesinmeyer"
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Niels H. Andersen grad student 2005 University of Washington
 (Chemical shifts define the structure and folding thermodynamics of polypeptides.)
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Publications

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Anderson JM, Kier B, Jurban B, et al. (2016) Aryl-Aryl interactions in designed peptide folds: Spectroscopic characteristics and placement issues for optimal structure stabilization. Biopolymers
Gokarn YR, Fesinmeyer RM, Saluja A, et al. (2009) Ion-specific modulation of protein interactions: anion-induced, reversible oligomerization of a fusion protein. Protein Science : a Publication of the Protein Society. 18: 169-79
Song K, Stewart JM, Fesinmeyer RM, et al. (2008) Structural insights for designed alanine-rich helices: comparing NMR helicity measures and conformational ensembles from molecular dynamics simulation. Biopolymers. 89: 747-60
Andersen NH, Olsen KA, Fesinmeyer RM, et al. (2006) Minimization and optimization of designed beta-hairpin folds. Journal of the American Chemical Society. 128: 6101-10
Fesinmeyer RM, Hudson FM, Olsen KA, et al. (2005) Chemical shifts provide fold populations and register of beta hairpins and beta sheets. Journal of Biomolecular Nmr. 33: 213-31
Olsen KA, Fesinmeyer RM, Stewart JM, et al. (2005) Hairpin folding rates reflect mutations within and remote from the turn region. Proceedings of the National Academy of Sciences of the United States of America. 102: 15483-7
Fesinmeyer RM, Peterson ES, Dyer RB, et al. (2005) Studies of helix fraying and solvation using 13C' isotopomers. Protein Science : a Publication of the Protein Society. 14: 2324-32
Dyer RB, Maness SJ, Franzen S, et al. (2005) Hairpin folding dynamics: the cold-denatured state is predisposed for rapid refolding. Biochemistry. 44: 10406-15
Dyer RB, Maness SJ, Peterson ES, et al. (2004) The mechanism of beta-hairpin formation. Biochemistry. 43: 11560-6
Fesinmeyer RM, Hudson FM, Andersen NH. (2004) Enhanced hairpin stability through loop design: the case of the protein G B1 domain hairpin. Journal of the American Chemical Society. 126: 7238-43
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