Related ArticlesAn investigation of the dynamics of ribosomal protein L9 using heteronuclear NMR relaxation measurements.
J Mol Biol. 1998 Aug 21;281(3):539-51
Authors: Lillemoen J, Hoffman DW
The dynamic properties of ribosomal protein L9 from Bacillus stearothermophilus were investigated in solution using an analysis of nitrogen-15 longitudinal and transverse relaxation rates and amide nitrogen-proton nuclear Overhauser effects. The relaxation rates of the amide nitrogen nuclei were found to be correlated with the angle between the amide nitrogen-proton bond vectors and the long axis of the protein. This directional dependence of the nuclear relaxation rates is consistent with the protein having a highly elongated shape in solution, consistent with that observed in previous X-ray crystallographic studies of the crystalline form. Analysis of the nuclear relaxation data shows that the solvent-exposed nine-turn alpha helix connecting the two domains has a relatively high degree of order, in contrast to the connecting helix in the similarly shaped, but functionally different, calmodulin protein. The rotational correlation times associated with the amide nitrogen atoms of the N-terminal domain are on average slightly shorter than those of the C-terminal domain and connecting helix, providing evidence that the N-terminal domain exhibits some degree of independence in tumbling, in addition to other fast internal motions. The putative RNA-binding surfaces in each of the protein domains are characterized by relatively low order parameters, indicating that these are the most flexible regions of the molecule. Overall, the picture of the internal dynamics provided by nuclear relaxation measurements is similar to that obtained from a detailed study of amide proton exchange rates, but differs markedly from the picture provided by crystallographic temperature factors. The present study describes a molecule with unusual and complex dynamic properties, and supports a model where the protein functions as a "molecular strut" within the ribosome.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear (1)H-(15)N NMR Spectroscopy.
J Am Chem Soc. 2010 Dec 27;
Authors: Esadze A, Li DW, Wang T, Bru?schweiler R, Iwahara J
Despite their importance in macromolecular interactions and functions, the dynamics of lysine side-chain amino groups in proteins are not well understood. In this study, we have developed the methodology for the investigations of the dynamics...
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Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Dynamics of Lysine Side-Chain Amino Groups in a Protein Studied by Heteronuclear 1H-15N NMR Spectroscopy
Alexandre Esadze, Da-Wei Li, Tianzhi Wang, Rafael Bru?schweiler and Junji Iwahara
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107847d/aop/images/medium/ja-2010-07847d_0007.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107847d
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/iFwgRBt-zto
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[NMR paper] Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR rela
Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: the possibility of obtaining long-range structure information.
Related Articles Binding ability of a HHP-tagged protein towards Ni2+ studied by paramagnetic NMR relaxation: the possibility of obtaining long-range structure information.
J Biomol NMR. 2004 Jun;29(2):175-85
Authors: Jensen MR, Lauritzen C, Dahl SW, Pedersen J, Led JJ
The binding ability of a protein with a metal binding tag towards Ni(2+) was investigated by longitudinal paramagnetic NMR...
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[NMR paper] Protein dynamics using frequency-dependent order parameters from analysis of NMR rela
Protein dynamics using frequency-dependent order parameters from analysis of NMR relaxation data.
Related Articles Protein dynamics using frequency-dependent order parameters from analysis of NMR relaxation data.
J Magn Reson. 2003 Mar;161(1):118-25
Authors: Idiyatullin D, Daragan VA, Mayo KH
A novel approach is described to analyze NMR relaxation data on proteins. This method introduces the frequency-dependent order parameter, S(2)(omega), in order to estimate contributions to the generalized order parameter S(2) from different motional...
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[NMR paper] Structure and dynamics of MarA-DNA complexes: an NMR investigation.
Structure and dynamics of MarA-DNA complexes: an NMR investigation.
Related Articles Structure and dynamics of MarA-DNA complexes: an NMR investigation.
J Mol Biol. 2001 Nov 16;314(1):113-27
Authors: Dangi B, Pelupessey P, Martin RG, Rosner JL, Louis JM, Gronenborn AM
An unanswered question regarding gene regulation is how certain proteins are capable of binding to DNA with high affinity at specific but highly degenerate consensus sequences. We have investigated the interactions between the Escherichia coli transcription factor, MarA, and its...
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[NMR paper] Comparison of backbone dynamics of oxidized and reduced putidaredoxin by 15N NMR rela
Comparison of backbone dynamics of oxidized and reduced putidaredoxin by 15N NMR relaxation measurements.
Related Articles Comparison of backbone dynamics of oxidized and reduced putidaredoxin by 15N NMR relaxation measurements.
Biochemistry. 1999 Aug 3;38(31):9862-71
Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B
The backbone dynamics of uniformly 15N-labeled reduced and oxidized putidaredoxin (Pdx) have been studied by 2D 15N NMR relaxation measurements. 15N T1 and T2 values and 1H-15N NOEs have been measured for the diamagnetic...
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[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
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Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
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[NMR paper] Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and
Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Related Articles Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.
Biochemistry. 1994 Mar 29;33(12):3515-31
Authors: Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED
A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the...
An investigation of the dynamics of ribosomal protein L9 using heteronuclear NMR rela
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