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Martin Blackledge

Showing results (31-40 of 205) with videos related to

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Biochemistry|March 11, 2011
Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scalesLoïc Salmon, Guillaume Bouvignies, Phineus Markwick, et al.
Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry|July 27, 2007
Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplingsGuillaume Bouvignies, Phineus R L Markwick, Martin Blackledge
Proteins|October 25, 2007
Characterization of protein dynamics from residual dipolar couplings using the three dimensional Gaussian axial fluctuation modelGuillaume Bouvignies, Phineus R L Markwick, Martin Blackledge
Journal of Magnetic Resonance (San Diego, Calif. : 1997)|February 7, 2007
The role of (15)N CSA and CSA/dipole cross-correlation in (15)N relaxation in solid proteinsJulien Sein, Nicolas Giraud, Martin Blackledge, et al.
Angewandte Chemie (International Ed. in English)|November 23, 2006
Ultrahigh-resolution backbone structure of perdeuterated protein GB1 using residual dipolar couplings from two alignment mediaGuillaume Bouvignies, Sebastian Meier, Stephan Grzesiek, et al.
Biophysical Journal|June 26, 2007
Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor PKlaartje Houben, Laurence Blanchard, Martin Blackledge, et al.
Journal of Magnetic Resonance (San Diego, Calif. : 1997)|October 13, 2006
The influence of nitrogen-15 proton-driven spin diffusion on the measurement of nitrogen-15 longitudinal relaxation timesNicolas Giraud, Martin Blackledge, Anja Böckmann, et al.
BMC Bioinformatics|April 10, 2009
ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensembleJorge Estrada, Pau Bernadó, Martin Blackledge, et al.
Current Opinion in Structural Biology|April 3, 2013
Describing intrinsically disordered proteins at atomic resolution by NMRMalene Ringkjøbing Jensen, Rob W H Ruigrok, Martin Blackledge
Journal of the American Chemical Society|November 18, 2009
Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteinsJózef R Lewandowski, Julien Sein, Martin Blackledge, et al.
Pageof 21

Showing results (31-40 of 205) with videos related to

Sort By:
Pageof 21
Biochemistry|March 11, 2011
Nuclear magnetic resonance provides a quantitative description of protein conformational flexibility on physiologically important time scalesLoïc Salmon, Guillaume Bouvignies, Phineus Markwick, et al.
Chemphyschem : a European Journal of Chemical Physics and Physical Chemistry|July 27, 2007
Simultaneous definition of high resolution protein structure and backbone conformational dynamics using NMR residual dipolar couplingsGuillaume Bouvignies, Phineus R L Markwick, Martin Blackledge
Proteins|October 25, 2007
Characterization of protein dynamics from residual dipolar couplings using the three dimensional Gaussian axial fluctuation modelGuillaume Bouvignies, Phineus R L Markwick, Martin Blackledge
Journal of Magnetic Resonance (San Diego, Calif. : 1997)|February 7, 2007
The role of (15)N CSA and CSA/dipole cross-correlation in (15)N relaxation in solid proteinsJulien Sein, Nicolas Giraud, Martin Blackledge, et al.
Angewandte Chemie (International Ed. in English)|November 23, 2006
Ultrahigh-resolution backbone structure of perdeuterated protein GB1 using residual dipolar couplings from two alignment mediaGuillaume Bouvignies, Sebastian Meier, Stephan Grzesiek, et al.
Biophysical Journal|June 26, 2007
Intrinsic dynamics of the partly unstructured PX domain from the Sendai virus RNA polymerase cofactor PKlaartje Houben, Laurence Blanchard, Martin Blackledge, et al.
Journal of Magnetic Resonance (San Diego, Calif. : 1997)|October 13, 2006
The influence of nitrogen-15 proton-driven spin diffusion on the measurement of nitrogen-15 longitudinal relaxation timesNicolas Giraud, Martin Blackledge, Anja Böckmann, et al.
BMC Bioinformatics|April 10, 2009
ProtSA: a web application for calculating sequence specific protein solvent accessibilities in the unfolded ensembleJorge Estrada, Pau Bernadó, Martin Blackledge, et al.
Current Opinion in Structural Biology|April 3, 2013
Describing intrinsically disordered proteins at atomic resolution by NMRMalene Ringkjøbing Jensen, Rob W H Ruigrok, Martin Blackledge
Journal of the American Chemical Society|November 18, 2009
Anisotropic collective motion contributes to nuclear spin relaxation in crystalline proteinsJózef R Lewandowski, Julien Sein, Martin Blackledge, et al.
Pageof 21