Stewart N. Loh
Affiliations: | 1987-1993 | Biochemistry | University of Wisconsin, Madison, Madison, WI |
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"Stewart Loh"Mean distance: 8.42 | S | N | B | C | P |
Children
Sign in to add trainee| Joshua Michael Karchin | grad student | SUNY Upstate Medical University | |
| Margaret Stratton | grad student | SUNY Upstate Medical University |
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| Stratton MM, McClendon S, Eliezer D, et al. (2011) Structural characterization of two alternate conformations in a calbindin D₉k-based molecular switch. Biochemistry. 50: 5583-9 |
| Stratton MM, Loh SN. (2011) Converting a protein into a switch for biosensing and functional regulation. Protein Science : a Publication of the Protein Society. 20: 19-29 |
| Stratton MM, Loh SN. (2010) On the mechanism of protein fold-switching by a molecular sensor. Proteins. 78: 3260-9 |
| Stratton MM, Cutler TA, Ha JH, et al. (2010) Probing local structural fluctuations in myoglobin by size-dependent thiol-disulfide exchange. Protein Science : a Publication of the Protein Society. 19: 1587-94 |
| Chen H, Stratton M, Loh SN, et al. (2009) Structural Fluctuations In Apomyoglobin Undergoing Transition To An Amyloid State Biophysical Journal. 96: 324a |
| Stratton MM, Mitrea DM, Loh SN. (2008) A Ca2+-sensing molecular switch based on alternate frame protein folding. Acs Chemical Biology. 3: 723-32 |
| Feng Z, Butler MC, Alam SL, et al. (2001) On the nature of conformational openings: Native and unfolded-state hydrogen and thiol-disulfide exchange studies of ferric aquomyoglobin Journal of Molecular Biology. 314: 153-166 |
| Feng Z, Ha JH, Loh SN. (1999) Identifying the site of initial tertiary structure disruption during apomyoglobin unfolding Biochemistry. 38: 14433-14439 |
| Ha JH, Loh SN. (1998) Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange Nature Structural Biology. 5: 730-737 |
| Loh SN, Rohl CA, Kiefhaber T, et al. (1996) A general two-process model describes the hydrogen exchange behavior of RNase A in unfolding conditions. Proceedings of the National Academy of Sciences of the United States of America. 93: 1982-7 |