Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a high degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations of these measurements from predictions based on available crystallographic and solution structures are largely systematic and well correlated within a given helix of this highly alpha-helical protein. These observations can be explained by invoking collective motion and small displacements of representative helices from their reported average positions in the solid state. Thus, the measurements appear to be capable of providing important insights into slower, collective protein motions, which are likely to be important for function, and which have been difficult to study using established experimental techniques.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Comparative analysis of essential collective dynamics and NMR-derived flexibility profiles in evolutionarily diverse prion proteins.
Prion. 2011 Jul 1;5(3)
Authors: Santo KP, Berjanskii M, Wishart DS, Stepanova M
Abstract
Collective motions on ns-?s time scales are known to have a major impact on protein folding, stability, binding and enzymatic efficiency. It is also believed that these motions may have an...
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[NMR paper] Characterization of the internal motions of a chimeric protein by 13C NMR highlights
Characterization of the internal motions of a chimeric protein by 13C NMR highlights the important dynamic consequences of the engineering on a millisecond time scale.
Related Articles Characterization of the internal motions of a chimeric protein by 13C NMR highlights the important dynamic consequences of the engineering on a millisecond time scale.
Eur J Biochem. 2000 Nov;267(22):6519-33
Authors: Wolff N, Guenneugues M, Gilquin B, Drakopoulou E, Vita C, Ménez A, Zinn-Justin S
By transferring the central curaremimetic beta hairpin of the...
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[NMR paper] Identification of slow motions in the reduced recombinant high-potential iron sulfur
Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
Related Articles Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.
J Biomol NMR. 1998 Aug;12(2):307-18
Authors: Banci L, Felli IC, Koulougliotis D
Rotating-frame 15N relaxation rate (R1 rho) NMR experiments have been...
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[NMR paper] NMR evidence for slow collective motions in cyanometmyoglobin.
NMR evidence for slow collective motions in cyanometmyoglobin.
Related Articles NMR evidence for slow collective motions in cyanometmyoglobin.
Nat Struct Biol. 1997 Apr;4(4):292-7
Authors: Tolman JR, Flanagan JM, Kennedy MA, Prestegard JH
Residual dipolar couplings observed in NMR spectra at very high magnetic fields have been measured to a high degree of accuracy for the paramagnetic protein cyanometmyoglobin. Deviations of these measurements from predictions based on available crystallographic and solution structures are largely systematic...
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[NMR paper] Collective NMR relaxation model applied to protein dynamics.
Collective NMR relaxation model applied to protein dynamics.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/-PMGifs-Toolbar-topub.gif Related Articles Collective NMR relaxation model applied to protein dynamics.
Phys Rev Lett. 1994 Feb 7;72(6):940-943
Authors: Brüschweiler R, Case DA
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[NMR paper] Collective NMR relaxation model applied to protein dynamics.
Collective NMR relaxation model applied to protein dynamics.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/-PMGifs-Toolbar-topub.gif Related Articles Collective NMR relaxation model applied to protein dynamics.
Phys Rev Lett. 1994 Feb 7;72(6):940-943
Authors: Brüschweiler R, Case DA
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[NMR paper] Solution structural characteristics of cyanometmyoglobin: resonance assignment of hem
Solution structural characteristics of cyanometmyoglobin: resonance assignment of heme cavity residues by two-dimensional NMR.
Related Articles Solution structural characteristics of cyanometmyoglobin: resonance assignment of heme cavity residues by two-dimensional NMR.
Biochemistry. 1990 Feb 13;29(6):1545-56
Authors: Emerson SD, La Mar G
Steady-state nuclear Overhauser effects (NOE), two-dimensional (2D) nuclear Overhauser effect spectroscopy (NOESY), and 2D spin correlation spectroscopy (COSY) have been applied to the fully paramagnetic...
NMR evidence for slow collective motions in cyanometmyoglobin.
Linear Mode
