Chimeric Avidin - NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable Protein.
PLoS One. 2014;9(6):e100564
Authors: Tossavainen H, Kukkurainen S, Määttä JA, Kähkönen N, Pihlajamaa T, Hytönen VP, Kulomaa MS, Permi P
Abstract
Chimeric avidin (ChiAVD) is a product of rational protein engineering remarkably resistant to heat and harsh conditions. In quest of the fundamentals behind factors affecting stability we have elucidated the solution NMR spectroscopic structure of the biotin-bound form of ChiAVD and characterized the protein dynamics through 15N relaxation and hydrogen/deuterium (H/D) exchange of this and the biotin-free form. To surmount the challenges arising from the very large size of the protein for NMR spectroscopy, we took advantage of its high thermostability. Conventional triple resonance experiments for fully protonated proteins combined with methyl-detection optimized experiments acquired at 58°C were adequate for the structure determination of this 56 kDa protein. The model-free parameters derived from the 15N relaxation data reveal a remarkably rigid protein at 58°C in both the biotin-bound and the free forms. The H/D exchange experiments indicate a notable increase in hydrogen protection upon biotin binding.
PMID: 24959850 [PubMed - as supplied by publisher]
[NMR paper] Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease.
Molecules. 2013;18(5):4929-41
Authors: Ramírez-Gualito K, Richter M, Matzapetakis M, Singer D, Berger S
Abstract
Rational design of peptide vaccines becomes important for the treatment of some diseases such as Alzheimer's disease (AD) and related disorders. In this study, as part of a larger...
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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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[NMR structure and dynamics of the chimeric protein SH3-F2].
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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...
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[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] 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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[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)...
Chimeric Avidin - NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable Protein.
Linear Mode
