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N K Goto

Showing results (1-10 of 9) with videos related to

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Current Opinion in Structural Biology|October 24, 2000
New developments in isotope labeling strategies for protein solution NMR spectroscopyN K Goto, L E Kay
Nature Structural Biology|October 1, 1996
Folding proteins into membranesC M Deber, N K Goto
Journal of Biomolecular NMR|December 8, 2010
An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled ProteinsD Yang, J R Tolman, N K Goto, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 25, 1996
Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environmentS C Li, N K Goto, K A Williams, et al.
Journal of Molecular Biology|May 15, 2001
What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMRN K Goto, N R Skrynnikov, F W Dahlquist, et al.
Biopolymers|September 1, 1996
Threshold hydrophobicity dictates helical conformations of peptides in membrane environmentsL P Liu, S C Li, N K Goto, et al.
Journal of Molecular Biology|June 12, 2001
Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopyJ Evenäs, V Tugarinov, N R Skrynnikov, et al.
Journal of Biomolecular NMR|June 26, 1999
A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteinsN K Goto, K H Gardner, G A Mueller, et al.
Journal of Molecular Biology|February 2, 2000
Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrinN R Skrynnikov, N K Goto, D Yang, et al.
Pageof 1

Showing results (1-10 of 9) with videos related to

Sort By:
Pageof 1
Current Opinion in Structural Biology|October 24, 2000
New developments in isotope labeling strategies for protein solution NMR spectroscopyN K Goto, L E Kay
Nature Structural Biology|October 1, 1996
Folding proteins into membranesC M Deber, N K Goto
Journal of Biomolecular NMR|December 8, 2010
An HNCO-based Pulse Scheme for the Measurement of 13Cα-1Hα One-bond Dipolar couplings in 15N, 13C Labeled ProteinsD Yang, J R Tolman, N K Goto, et al.
Proceedings of the National Academy of Sciences of the United States of America|June 25, 1996
Alpha-helical, but not beta-sheet, propensity of proline is determined by peptide environmentS C Li, N K Goto, K A Williams, et al.
Journal of Molecular Biology|May 15, 2001
What is the average conformation of bacteriophage T4 lysozyme in solution? A domain orientation study using dipolar couplings measured by solution NMRN K Goto, N R Skrynnikov, F W Dahlquist, et al.
Biopolymers|September 1, 1996
Threshold hydrophobicity dictates helical conformations of peptides in membrane environmentsL P Liu, S C Li, N K Goto, et al.
Journal of Molecular Biology|June 12, 2001
Ligand-induced structural changes to maltodextrin-binding protein as studied by solution NMR spectroscopyJ Evenäs, V Tugarinov, N R Skrynnikov, et al.
Journal of Biomolecular NMR|June 26, 1999
A robust and cost-effective method for the production of Val, Leu, Ile (delta 1) methyl-protonated 15N-, 13C-, 2H-labeled proteinsN K Goto, K H Gardner, G A Mueller, et al.
Journal of Molecular Biology|February 2, 2000
Orienting domains in proteins using dipolar couplings measured by liquid-state NMR: differences in solution and crystal forms of maltodextrin binding protein loaded with beta-cyclodextrinN R Skrynnikov, N K Goto, D Yang, et al.
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