Related ArticlesSolution NMR Spectroscopy for the Study of Enzyme Allostery.
Chem Rev. 2016 Jan 6;
Authors: Lisi GP, Loria JP
Abstract
Allostery is a ubiquitous biological regulatory process in which distant binding sites within a protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions play essential roles in many enzymological mechanisms, often facilitating formation of enzyme-substrate complexes and/or product release. Thus, elucidating the forces that drive allostery is critical to understanding the complex transformations of biomolecules. Currently, a number of models exist to describe allosteric behavior, taking into account energetics as well as conformational rearrangements and fluctuations. In the following Review, we discuss the use of solution NMR techniques designed to probe allosteric mechanisms in enzymes. NMR spectroscopy is unequaled in its ability to detect structural and dynamical changes in biomolecules, and the case studies presented herein demonstrate the range of insights to be gained from this valuable method. We also provide a detailed technical discussion of several specialized NMR experiments that are ideally suited for the study of enzymatic allostery.
PMID: 26734986 [PubMed - as supplied by publisher]
[NMR paper] Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.
Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.
Solution NMR Spectroscopy Provides an Avenue for the Study of Functionally Dynamic Molecular Machines: The Example of Protein Disaggregation.
J Am Chem Soc. 2015 Dec 11;
Authors: Rosenzweig R, Kay LE
Abstract
Solution-based NMR spectroscopy has been an important tool for studying the structure and dynamics of relatively small proteins and protein complexes with aggregate molecular masses...
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12-15-2015 08:09 PM
[NMR paper] The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Related Articles The study of transient protein-nanoparticle interactions by solution NMR spectroscopy.
Biochim Biophys Acta. 2015 Apr 30;
Authors: Assfalg M, Ragona L, Pagano K, D'Onofrio M, Zanzoni S, Tomaselli S, Molinari H
Abstract
The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nano-bio interfaces. Nanoparticles exhibit unique structures and properties, often...
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The study of transient protein-nanoparticle interactions by solution NMR spectroscopy
The study of transient protein-nanoparticle interactions by solution NMR spectroscopy
Publication date: Available online 30 April 2015
Source:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics</br>
Author(s): Michael Assfalg , Laura Ragona , Katiuscia Pagano , Mariapina D’Onofrio , Serena Zanzoni , Simona Tomaselli , Henriette Molinari</br>
The rapid development of novel nanoscale materials for applications in biomedicine urges an improved characterization of the nano-bio interfaces. Nanoparticles exhibit unique structures and properties, often...
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04-30-2015 09:13 PM
A Novel Tri-Enzyme System in Combination with Laser-Driven NMR Enables Efficient Nuclear Polarization of Biomolecules in Solution
From The DNP-NMR Blog:
A Novel Tri-Enzyme System in Combination with Laser-Driven NMR Enables Efficient Nuclear Polarization of Biomolecules in Solution
Lee, J.H. and S. Cavagnero, A Novel Tri-Enzyme System in Combination with Laser-Driven NMR Enables Efficient Nuclear Polarization of Biomolecules in Solution. The Journal of Physical Chemistry B, 2013. 117(20): p. 6069-6081.
http://dx.doi.org/10.1021/jp4010168
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07-10-2013 05:30 PM
[NMR paper] Solution NMR and Computational Methods for Understanding Protein Allostery.
Solution NMR and Computational Methods for Understanding Protein Allostery.
Solution NMR and Computational Methods for Understanding Protein Allostery.
J Phys Chem B. 2013 Feb 26;
Authors: Manley GA, Rivalta I, Loria JP
Abstract
Allosterism is an essential biological regulatory mechanism. In enzymes, allosteric regulation results in an activation or inhibition of catalytic turnover. The mechanisms by which this is accomplished are unclear and vary significantly depending on the enzyme. It is commonly the case that a metabolite binds to...
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03-01-2013 09:57 PM
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
...
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08-22-2010 03:31 PM
[NMR paper] Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia col
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR.
Biochemistry. 1997 Mar 4;36(9):2517-30
Authors: Garrett DS, Seok YJ, Liao DI, Peterkofsky A, Gronenborn AM, Clore GM
...
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08-22-2010 03:03 PM
NMR post-doc position: NMR-based dynamics study of enzyme mechanism
The following post-doc position in NMR is available in University of Missouri:
Ad text:
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We have an opening for a postdoctoral fellow to use NMR to study dynamics of an enzyme while it is carrying on reversible catalysis. The prospects are promising and can be compared with thorough enzymology and crystallography of its ligand-dependent conformational changes (done in our dept.). The enzyme is sizeable enough to be challenging, but we have a battery of excellent 800 MHz spectra of deuterated samples for launching the project. The postdoctoral fellow will be housed in a new...
Solution NMR Spectroscopy for the Study of Enzyme Allostery.
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