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Current Opinion in Structural Biology
|
October 24, 2000
New developments in isotope labeling strategies for protein solution NMR spectroscopy
N K Goto, L E Kay
Nature Structural Biology
|
October 1, 1996
Folding proteins into membranes
C 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 Proteins
D 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 environment
S 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 NMR
N K Goto, N R Skrynnikov, F W Dahlquist, et al.
Biopolymers
|
September 1, 1996
Threshold hydrophobicity dictates helical conformations of peptides in membrane environments
L 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 spectroscopy
J 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 proteins
N 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-cyclodextrin
N R Skrynnikov, N K Goto, D Yang, et al.
Page
of 1
Search research articles
Search
Showing results (1-10 of 9) with videos related to
Sort By:
Page
of 1
Current Opinion in Structural Biology
|
October 24, 2000
New developments in isotope labeling strategies for protein solution NMR spectroscopy
N K Goto, L E Kay
Nature Structural Biology
|
October 1, 1996
Folding proteins into membranes
C 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 Proteins
D 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 environment
S 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 NMR
N K Goto, N R Skrynnikov, F W Dahlquist, et al.
Biopolymers
|
September 1, 1996
Threshold hydrophobicity dictates helical conformations of peptides in membrane environments
L 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 spectroscopy
J 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 proteins
N 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-cyclodextrin
N R Skrynnikov, N K Goto, D Yang, et al.
Page
of 1