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Stewart N. Loh - Publications

Affiliations: 
1987-1993 Biochemistry University of Wisconsin, Madison, Madison, WI 
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27 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2011 Stratton MM, McClendon S, Eliezer D, Loh SN. Structural characterization of two alternate conformations in a calbindin D₉k-based molecular switch. Biochemistry. 50: 5583-9. PMID 21618991 DOI: 10.1021/Bi102040G  0.593
2011 Stratton MM, Loh SN. Converting a protein into a switch for biosensing and functional regulation. Protein Science : a Publication of the Protein Society. 20: 19-29. PMID 21064163 DOI: 10.1002/pro.541  0.579
2010 Stratton MM, Loh SN. On the mechanism of protein fold-switching by a molecular sensor. Proteins. 78: 3260-9. PMID 20806404 DOI: 10.1002/prot.22833  0.601
2010 Stratton MM, Cutler TA, Ha JH, Loh SN. Probing local structural fluctuations in myoglobin by size-dependent thiol-disulfide exchange. Protein Science : a Publication of the Protein Society. 19: 1587-94. PMID 20572017 DOI: 10.1002/pro.440  0.597
2009 Chen H, Stratton M, Loh SN, Webb WW. Structural Fluctuations In Apomyoglobin Undergoing Transition To An Amyloid State Biophysical Journal. 96: 324a. DOI: 10.1016/J.Bpj.2008.12.1626  0.558
2008 Stratton MM, Mitrea DM, Loh SN. A Ca2+-sensing molecular switch based on alternate frame protein folding. Acs Chemical Biology. 3: 723-32. PMID 18947182 DOI: 10.1021/cb800177f  0.599
2001 Feng Z, Butler MC, Alam SL, Loh SN. 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. PMID 11724540 DOI: 10.1006/jmbi.2001.5117  0.326
1999 Feng Z, Ha JH, Loh SN. Identifying the site of initial tertiary structure disruption during apomyoglobin unfolding Biochemistry. 38: 14433-14439. PMID 10545165 DOI: 10.1021/bi991933e  0.327
1998 Ha JH, Loh SN. Changes in side chain packing during apomyoglobin folding characterized by pulsed thiol-disulfide exchange Nature Structural Biology. 5: 730-737. PMID 9699638 DOI: 10.1038/1436  0.314
1996 Loh SN, Rohl CA, Kiefhaber T, Baldwin RL. 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. PMID 8700871 DOI: 10.1073/Pnas.93.5.1982  0.394
1996 Shan SO, Loh S, Herschlag D. The energetics of hydrogen bonds in model systems: implications for enzymatic catalysis. Science (New York, N.Y.). 272: 97-101. PMID 8600542 DOI: 10.1126/Science.272.5258.97  0.408
1996 Prehoda KE, Loh SN, Markley JL. Modeling Volume Changes in Proteins Using Partial Molar Volumes of Model Compounds Techniques in Protein Chemistry. 7: 433-438. DOI: 10.1016/S1080-8914(96)80047-0  0.648
1995 Loh SN, Kay MS, Baldwin RL. Structure and stability of a second molten globule intermediate in the apomyoglobin folding pathway Proceedings of the National Academy of Sciences of the United States of America. 92: 5446-5450. PMID 7777528 DOI: 10.1073/Pnas.92.12.5446  0.42
1994 Loh SN, Markley JL. Hydrogen bonding in proteins as studied by amide hydrogen D/H fractionation factors: application to staphylococcal nuclease. Biochemistry. 33: 1029-36. PMID 8305430 DOI: 10.1021/Bi00170A023  0.582
1994 Markley JL, Prehoda K, Truckses D, Wang J, Hinck AP, Loh SN, Walkenhorst WF. Case study of protein structure, stability, and function: NMR investigations of the proline residues in staphylococcal nuclease Pure and Applied Chemistry. 66: 65-69. DOI: 10.1351/Pac199466010065  0.621
1994 Loh SN, Prehoda KE, Wang J, Markley JL. Measuring Global and Local Structural Free Energy Changes in Staphylococcal Nuclease by NMR-Observed Hydrogen Exchange Techniques in Protein Chemistry. 5: 431-438. DOI: 10.1016/B978-0-12-194710-1.50053-9  0.745
1993 Eberhardt ES, Loh SN, Raines RT. Thermodynamic Origin of Prolyl Peptide Bond Isomers. Tetrahedron Letters. 34: 3055-3056. PMID 20628473 DOI: 10.1016/S0040-4039(00)93377-X  0.434
1993 Royer CA, Hinck AP, Loh SN, Prehoda KE, Peng X, Jonas J, Markley JL. Effects of amino acid substitutions on the pressure denaturation of staphylococcal nuclease as monitored by fluorescence and nuclear magnetic resonance spectroscopy. Biochemistry. 32: 5222-32. PMID 8494899 DOI: 10.1021/Bi00070A034  0.758
1993 Loh SN, Prehoda KE, Wang J, Markley JL. Hydrogen exchange in unligated and ligated staphylococcal nuclease. Biochemistry. 32: 11022-8. PMID 8218167 DOI: 10.1021/Bi00092A011  0.72
1993 Loh SN, Markley JL. Measurement of Amide Hydrogen D/H Fractionation Factors in Proteins by NMR Spectroscopy Techniques in Protein Chemistry. 517-524. DOI: 10.1016/B978-0-12-058757-5.50061-5  0.546
1992 Eberhardt ES, Loh SN, Hinck AP, Raines RT. Solvent Effects on the Energetics of Prolyl Peptide Bond Isomerization. Journal of the American Chemical Society. 114: 5437-5439. PMID 21451730 DOI: 10.1021/Ja00039A072  0.692
1992 Wang JF, Hinck AP, Loh SN, LeMaster DM, Markley JL. Solution studies of staphylococcal nuclease H124L. 2. 1H, 13C, and 15N chemical shift assignments for the unligated enzyme and analysis of chemical shift changes that accompany formation of the nuclease-thymidine 3',5'-bisphosphate-calcium ternary complex. Biochemistry. 31: 921-36. PMID 1731949 DOI: 10.1021/Bi00118A039  0.682
1990 Wang JF, Hinck AP, Loh SN, Markley JL. Two-dimensional NMR studies of staphylococcal nuclease: evidence for conformational heterogeneity from hydrogen-1, carbon-13, and nitrogen-15 spin system assignments of the aromatic amino acids in the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+ ternary complex. Biochemistry. 29: 4242-53. PMID 2361141 DOI: 10.1021/Bi00469A029  0.697
1990 Wang JF, Hinck AP, Loh SN, Markley JL. Two-dimensional NMR studies of staphylococcal nuclease. 2. Sequence-specific assignments of carbon-13 and nitrogen-15 signals from the nuclease H124L-thymidine 3',5'-bisphosphate-Ca2+ ternary complex. Biochemistry. 29: 102-13. PMID 2322533 DOI: 10.1021/Bi00453A012  0.688
1990 Hinck AP, Loh SN, Wang J, Markley JL. Histidine 121 of staphylococcal nuclease. Correction of the H(δ2) 1H NMR assignment and reinterpretation of the role this residue plays in conformational heterogeneity of the protein Journal of the American Chemical Society. 112: 9031-9034. DOI: 10.1021/Ja00181A001  0.634
1990 Alexandrescu AT, Loh SN, Markley JL. Chemical exchange spectroscopy based on carbon-13 NMR. Applications to enzymology and protein folding Journal of Magnetic Resonance (1969). 87: 523-535. DOI: 10.1016/0022-2364(90)90309-W  0.673
1990 Hinck AP, Loh SN, Wang J, Markley JL. Histidine 121 of staphylococcal nuclease. Correction of the Hδ2 1H NMR assignment and reinterpretation of the role this residue plays in conformational heterogeneity of the protein Journal of the American Chemical Society. 112.  0.64
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