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Results: 1-7 |
Results: 7
Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein
Authors: Choy, WY Tollinger, M Mueller, GA Kay, LE
Citation: Wy. Choy et al., Direct structure refinement of high molecular weight proteins against residual dipolar couplings and carbonyl chemical shift changes upon alignment: an application to maltose binding protein, J BIOM NMR, 21(1), 2001, pp. 31-40
Calculation of ensembles of structures representing the unfolded state of an SH3 domain
Authors: Choy, WY Forman-Kay, JD
Citation: Wy. Choy et Jd. Forman-kay, Calculation of ensembles of structures representing the unfolded state of an SH3 domain, J MOL BIOL, 308(5), 2001, pp. 1011-1032
Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy
Authors: Donaldson, LW Skrynnikov, NR Choy, WY Muhandiram, DR Sarkar, B Forman-Kay, JD Kay, LE
Citation: Lw. Donaldson et al., Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy, J AM CHEM S, 123(40), 2001, pp. 9843-9847
A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment
Authors: Mueller, GA Choy, WY Skrynnikov, NR Kay, LE
Citation: Ga. Mueller et al., A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment, J BIOM NMR, 18(3), 2000, pp. 183-188
Global folds of proteins with low densities of NOEs using residual dipolarcouplings: Application to the 370-residue maltodextrin-binding protein
Authors: Mueller, GA Choy, WY Yang, DW Forman-Kay, JD Venters, RA Kay, LE
Citation: Ga. Mueller et al., Global folds of proteins with low densities of NOEs using residual dipolarcouplings: Application to the 370-residue maltodextrin-binding protein, J MOL BIOL, 300(1), 2000, pp. 197-212
Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin bindingprotein loaded with beta-cyclodextrin
Authors: Skrynnikov, NR Goto, NK Yang, DW Choy, WY Tolman, JR Mueller, GA Kay, LE
Citation: Nr. Skrynnikov et al., Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: Differences in solution and crystal forms of maltodextrin bindingprotein loaded with beta-cyclodextrin, J MOL BIOL, 295(5), 2000, pp. 1265-1273
TROSY-based HNCO pulse sequences for the measurement of (HN)-H-1-N-15, N-15-(CO)-C-13, (HN)-H-1-(CO)-C-13, (CO)-C-13-C-13(alpha) and (HN)-H-1-C-13(alpha) dipolar couplings in N-15, C-13, H-2-labeled proteins
Authors: Yang, DW Venters, RA Mueller, GA Choy, WY Kay, LE
Citation: Dw. Yang et al., TROSY-based HNCO pulse sequences for the measurement of (HN)-H-1-N-15, N-15-(CO)-C-13, (HN)-H-1-(CO)-C-13, (CO)-C-13-C-13(alpha) and (HN)-H-1-C-13(alpha) dipolar couplings in N-15, C-13, H-2-labeled proteins, J BIOM NMR, 14(4), 1999, pp. 333-343
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