James M. Stewart, Ph.D. - Publications
Affiliations: | University of Washington, Seattle, Seattle, WA |
Area:
biorecognitionYear | Citation | Score | |||
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2013 | Shu I, Scian M, Stewart JM, Kier BL, Andersen NH. 13C structuring shifts for the analysis of model β-hairpins and β-sheets in proteins: diagnostic shifts appear only at the cross-strand H-bonded residues. Journal of Biomolecular Nmr. 56: 313-29. PMID 23851979 DOI: 10.1007/S10858-013-9749-3 | 0.674 | |||
2011 | Williams DV, Byrne A, Stewart J, Andersen NH. Optimal salt bridge for Trp-cage stabilization. Biochemistry. 50: 1143-52. PMID 21222485 DOI: 10.1021/Bi101555Y | 0.616 | |||
2011 | Shu I, Stewart JM, Scian M, Kier BL, Andersen NH. β-Sheet 13C structuring shifts appear only at the H-bonded sites of hairpins. Journal of the American Chemical Society. 133: 1196-9. PMID 21214243 DOI: 10.1021/Ja1088953 | 0.68 | |||
2008 | Stewart JM, Lin JC, Andersen NH. Lysine and arginine residues do not increase the helicity of alanine-rich peptide helices. Chemical Communications (Cambridge, England). 4765-7. PMID 18830486 DOI: 10.1039/B807101B | 0.662 | |||
2008 | Song K, Stewart JM, Fesinmeyer RM, Andersen NH, Simmerling C. Structural insights for designed alanine-rich helices: comparing NMR helicity measures and conformational ensembles from molecular dynamics simulation. Biopolymers. 89: 747-60. PMID 18428207 DOI: 10.1002/Bip.21004 | 0.707 | |||
2005 | Olsen KA, Fesinmeyer RM, Stewart JM, Andersen NH. 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. PMID 16227442 DOI: 10.1073/Pnas.0504392102 | 0.66 | |||
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