Related ArticlesBackbone dynamics of the cytotoxic ribonuclease alpha-sarcin by 15N NMR relaxation methods.
J Biomol NMR. 2002 Dec;24(4):301-16
Authors: Pérez-Cañadillas JM, Guenneugues M, Campos-Olivas R, Santoro J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
The cytotoxic ribonuclease alpha-sarcin is a 150-residue protein that inactivates ribosomes by selectively cleaving a single phosphodiester bond in a strictly conserved rRNA loop. In order to gain insights on the molecular basis of its highly specific activity, we have previously determined its solution structure and studied its electrostatics properties. Here, we complement those studies by analysing the backbone dynamics of alpha-sarcin through measurement of longitudinal relaxation rates R1, off resonance rotating frame relaxation rates R1 rho, and the 15N[1H] NOE of the backbone amide 15N nuclei at two different magnetic field strengths (11.7 and 17.6 T). The two sets of relaxation parameters have been analysed in terms of the reduced spectral density mapping formalism, as well as by the model-free approach. alpha-Sarcin behaves as an axial symmetric rotor of the prolate type (D(axially)/D(radially)=1.16 +/- 0.02) which tumbles with a correlation time tau(m) of 7.54 +/- 0.02 ns. The rotational diffusion properties have been also independently evaluated by hydrodynamic calculations and are in good agreement with the experimental results. The analysis of the internal dynamics reveals that alpha-sarcin is composed of a rigid hydrophobic core and some exposed segments which undergo fast (ps to ns) internal motions. Slower motions in the mu s to ms time scale are less abundant and in some cases can be assigned to specific motional processes. All dynamic data are discussed in relation to the role of some particular residues of alpha-sarcin in the process of recognition of its ribosomal target.
[NMR paper] Refined NMR structure of alpha-sarcin by 15N-1H residual dipolar couplings.
Refined NMR structure of alpha-sarcin by 15N-1H residual dipolar couplings.
Related Articles Refined NMR structure of alpha-sarcin by 15N-1H residual dipolar couplings.
Eur Biophys J. 2005 Nov;34(8):1057-65
Authors: García-Mayoral MF, Pantoja-Uceda D, Santoro J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
(15)N-(1)H residual dipolar couplings (RDC) have been used as additional restraints to refine the solution structure of the ribotoxin alpha-sarcin. The RDC values were obtained by partial alignment of alpha-sarcin in the binary mixture...
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[NMR paper] NMR structure of the noncytotoxic alpha-sarcin mutant Delta(7-22): the importance of
NMR structure of the noncytotoxic alpha-sarcin mutant Delta(7-22): the importance of the native conformation of peripheral loops for activity.
Related Articles NMR structure of the noncytotoxic alpha-sarcin mutant Delta(7-22): the importance of the native conformation of peripheral loops for activity.
Protein Sci. 2004 Apr;13(4):1000-11
Authors: García-Mayoral MF, García-Ortega L, Lillo MP, Santoro J, Martínez del Pozo A, Gavilanes JG, Rico M, Bruix M
The deletion mutant Delta(7-22) of alpha-sarcin, unlike its wild-type protein counterpart,...
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11-24-2010 09:51 PM
[NMR paper] Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implicati
Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
Related Articles Backbone dynamics of the human MIA protein studied by (15)N NMR relaxation: implications for extended interactions of SH3 domains.
Protein Sci. 2003 Mar;12(3):510-9
Authors: Stoll R, Renner C, Buettner R, Voelter W, Bosserhoff AK, Holak TA
The melanoma inhibitory activity (MIA) protein is a clinically valuable marker in patients with malignant melanoma as enhanced values diagnose metastatic...
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[NMR paper] Backbone dynamics of the ribonuclease binase active site area using multinuclear ((15
Backbone dynamics of the ribonuclease binase active site area using multinuclear ((15)N and (13)CO) NMR relaxation and computational molecular dynamics.
Related Articles Backbone dynamics of the ribonuclease binase active site area using multinuclear ((15)N and (13)CO) NMR relaxation and computational molecular dynamics.
Biochemistry. 2002 Feb 26;41(8):2655-66
Authors: Pang Y, Buck M, Zuiderweg ER
The nano-pico second backbone dynamics of the ribonuclease binase, homologous to barnase, is investigated with (15)N, (13)C NMR relaxation at 11.74...
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[NMR paper] Characterization of pKa values and titration shifts in the cytotoxic ribonuclease alp
Characterization of pKa values and titration shifts in the cytotoxic ribonuclease alpha-sarcin by NMR. Relationship between electrostatic interactions, structure, and catalytic function.
Related Articles Characterization of pKa values and titration shifts in the cytotoxic ribonuclease alpha-sarcin by NMR. Relationship between electrostatic interactions, structure, and catalytic function.
Biochemistry. 1998 Nov 10;37(45):15865-76
Authors: Pérez-Cañadillas JM, Campos-Olivas R, Lacadena J, Martínez del Pozo A, Gavilanes JG, Santoro J, Rico M, Bruix M
...
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[NMR paper] Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Backbone dynamics of the c-Jun leucine zipper: 15N NMR relaxation studies.
Biochemistry. 1996 Apr 16;35(15):4867-77
Authors: MacKay JP, Shaw GL, King GF
The backbone dynamics of the coiled-coil leucine zipper domain of c-Jun have been studied using proton-detected two-dimensional 1H-15N NMR spectroscopy. Longitudinal (T1) and transverse (T2) 15N relaxation times,...
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[NMR paper] Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Related Articles Backbone dynamics of trp repressor studied by 15N NMR relaxation.
Biochemistry. 1995 Apr 18;34(15):5212-23
Authors: Zheng Z, Czaplicki J, Jardetzky O
Backbone dynamics of trp repressor, a 25 kDa DNA binding protein, have been studied using 15N relaxation data measured by proton-detected two-dimensional 1H-15N NMR spectroscopy. 15N spin-lattice relaxation time (T1), spin-spin relaxation time (T2), and heteronuclear NOEs were determined for all visible backbone...
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[NMR paper] Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N
Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Relaxation study of the backbone dynamics of human profilin by two-dimensional 1H-15N NMR.
FEBS Lett. 1993 Dec 28;336(3):457-61
Authors: Constantine KL, Friedrichs MS, Bell AJ, Lavoie TB, Mueller L, Metzler WJ
The dynamic properties of 111 backbone HN sites in uncomplexed human profilin, a protein of 139 residues, have been...
Backbone dynamics of the cytotoxic ribonuclease alpha-sarcin by 15N NMR relaxation me
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