[NMR structure and dynamics of the chimeric protein SH3-F2].
Mol Biol (Mosk). 2010 Nov-Dec;44(6):1064-74
Authors:
For the further elucidation of structural and dynamic principles of protein self-organization and protein-ligand interactions the design of new chimeric protein SH3-F2 was made and genetically engineered construct was created. The SH3-F2 amino acid sequence consists of polyproline ligand mgAPPLPPYSA, GG linker and the sequence of spectrin SH3 domain circular permutant S19-P20s. Structural and dynamics properties of the protein were studied by high-resolution NMR. According to NMR data the tertiary structure of the chimeric protein SH3-F2 has the topology which is typical of SH3 domains in the complex with the ligand, forming polyproline type II helix, located in the conservative region of binding in the orientation II. The polyproline ligand closely adjoins with the protein globule and is stabilized by hydrophobic interactions. However the interaction of ligand and the part of globule relative to SH3 domain is not too large because the analysis of protein dynamic characteristics points to the low amplitude, high-frequency ligand tumbling in relation to the slow intramolecular motions of the main globule. The constructed chimera permits to carry out further structural and thermodynamic investigations of polyproline helix properties and its interaction with regulatory domains.
NMR studies of protein structure and dynamics
NMR studies of protein structure and dynamics
Publication year: 2011
Source: Journal of Magnetic Resonance, Volume 213, Issue 2, December 2011, Pages 477-491</br>
Lewis E.*Kay</br>
Recent advances in solution NMR spectroscopy have significantly extended the spectrum of problems that can now be addressed with this technology. In particular, studies of proteins with molecular weights on the order of 100*kDa are now possible at a level of detail that was previously reserved for much smaller systems. An example of the sort of information that is now accessible is provided in a study of...
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Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Structure, Dynamics, and Kinetics of Weak Protein-Protein Complexes from NMR Spin Relaxation Measurements of Titrated Solutions.
Angew Chem Int Ed Engl. 2011 Mar 18;
Authors: Salmon L, Ortega Roldan JL, Lescop E, Licinio A, van Nuland N, Jensen MR, Blackledge M
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03-23-2011 05:41 PM
[NMR paper] NMR studies of protein structure and dynamics.
NMR studies of protein structure and dynamics.
Related Articles NMR studies of protein structure and dynamics.
J Magn Reson. 2005 Apr;173(2):193-207
Authors: Kay LE
Recent advances in solution NMR spectroscopy have significantly extended the spectrum of problems that can now be addressed with this technology. In particular, studies of proteins with molecular weights on the order of 100 kDa are now possible at a level of detail that was previously reserved for much smaller systems. An example of the sort of information that is now accessible is...
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11-25-2010 08:21 PM
[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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11-19-2010 08:29 PM
[NMR paper] Relationships between protein structure and dynamics from a database of NMR-derived b
Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters.
Related Articles Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters.
J Mol Biol. 2000 Jan 28;295(4):963-78
Authors: Goodman JL, Pagel MD, Stone MJ
The amplitude of protein backbone NH group motions on a time-scale faster than molecular tumbling may be determined by analysis of (15)N NMR relaxation data according to the Lipari-Szabo model free formalism. An internet-accessible...
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11-18-2010 09:15 PM
[NMR paper] Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domai
Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: comparison to a related immunogenic peptide from HIV-1 RF.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformational preferences of a chimeric peptide HIV-1 immunogen from the C4-V3 domains of gp120 envelope protein of HIV-1 CAN0A based on solution NMR: comparison to a related immunogenic peptide from HIV-1 RF.
Biochemistry. 1996 Apr 23;35(16):5158-65
...
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08-22-2010 02:27 PM
[NMR paper] Solution structure by 2D 1H-NMR of a chimeric peptide recognized by galanin and neuro
Solution structure by 2D 1H-NMR of a chimeric peptide recognized by galanin and neuropeptide Y receptors.
Related Articles Solution structure by 2D 1H-NMR of a chimeric peptide recognized by galanin and neuropeptide Y receptors.
Biochemistry. 1993 Aug 3;32(30):7787-98
Authors: Arvidsson K, Land T, Langel U, Bartfai T, Ehrenberg A
The 25 amino acid residue chimeric peptide M32, galanin(1-13)-neuropeptide Y(25-36)-amide, was synthesized. The peptide was found to be recognized by both galanin and NPY receptors. The solution structure in 30% (v/v)...
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Paramagnetic tagging for protein structure and dynamics analysis
Paramagnetic tagging for protein structure and dynamics analysis
Publication year: 2010
Source: Progress in Nuclear Magnetic Resonance Spectroscopy, In Press, Accepted Manuscript, Available online 12 August 2010</br>
Peter H.J., Keizers , Marcellus, Ubbink</br>
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