Related ArticlesUsing Singular Value Decomposition to Characterize Protein-Protein Interactions by In-cell NMR Spectroscopy.
Chembiochem. 2014 Apr 1;
Authors: Majumder S, Demott CM, Burz DS, Shekhtman A
Abstract
Distinct differences between how model proteins interact in-cell and in vitro suggest that the cytosol might have a profound effect in modulating protein-protein and/or protein-ligand interactions that are not observed in vitro. Analyses of in-cell NMR spectra of target proteins interacting with physiological partners are further complicated by low signal-to-noise ratios, and the long overexpression times used in protein-protein interaction studies may lead to changes in the in-cell spectra over the course of the experiment. To unambiguously resolve the principal binding mode between two interacting species against the dynamic cellular background, we analyzed in-cell spectral data of a target protein over the time course of overexpression of its interacting partner by using single-value decomposition (SVD). SVD differentiates between concentration-dependent and concentration-independent events and identifies the principal binding mode between the two species. The analysis implicates a set of amino acids involved in the specific interaction that differs from previous NMR analyses but is in good agreement with crystallographic data.
PMID: 24692227 [PubMed - as supplied by publisher]
[NMR paper] Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Related Articles Revealing Cell-Surface Intramolecular Interactions in the BlaR1 Protein of Methicillin-Resistant Staphylococcus aureus by NMR Spectroscopy.
Biochemistry. 2013 Dec 20;
Authors: Frederick TE, Wilson BD, Cha J, Mobashery S, Peng JW
Abstract
In methicillin-resistant Staphylococcus aureus, ?-lactam antibiotic resistance is mediated by the transmembrane protein BlaR1. The antibiotic-sensor...
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12-24-2013 01:04 PM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these interactions...
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09-30-2011 06:00 AM
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Exploring weak, transient protein-protein interactions in crowded in vivo environments by in-cell NMR spectroscopy.
Biochemistry. 2011 Sep 26;
Authors: Wang Q, Zhuravleva A, Gierasch LM
Abstract
Biology relies on functional interplay of proteins in the crowded and heterogeneous environment inside cells, and functional protein interactions are often weak and transient. Thus, methods are needed that preserve these...
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09-30-2011 05:59 AM
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Protein Interactions in the Escherichia coli Cytosol: An Impediment to In-Cell NMR Spectroscopy.
Chembiochem. 2011 Mar 29;
Authors: Crowley PB, Chow E, Papkovskaia T
Protein science is shifting towards experiments performed under native or native-like conditions. In-cell NMR spectroscopy for instance has the potential to reveal protein structure and dynamics inside cells. However, not all proteins can be studied by this technique. (15) N-labelled...
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03-31-2011 06:24 PM
[NMR paper] Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Related Articles Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
J Biomol NMR. 2005 Jul;32(3):235-41
Authors: Ozawa K, Jergic S, Crowther JA, Thompson PR, Wijffels G, Otting G, Dixon NA
Cell-free protein synthesis systems provide facile access to proteins in a nascent state that enables formation of soluble, native protein-protein complexes even if one of the protein components is prone...
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12-01-2010 06:56 PM
[NMR paper] Use of selective Trp side chain labeling to characterize protein-protein and protein-
Use of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
Related Articles Use of selective Trp side chain labeling to characterize protein-protein and protein-ligand interactions by NMR spectroscopy.
J Am Chem Soc. 2003 Mar 12;125(10):2892-3
Authors: Rodriguez-Mias RA, Pellecchia M
Recent studies on amino acid occurrence in protein binding sites suggest that only a reduced number of residues are responsible for most interaction energy in protein-protein and protein-ligand...
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11-24-2010 09:01 PM
[NMR paper] Spin labels as a tool to identify and characterize protein-ligand interactions by NMR
Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy.
Related Articles Spin labels as a tool to identify and characterize protein-ligand interactions by NMR spectroscopy.
Chembiochem. 2002 Mar 1;3(2-3):167-73
Authors: Jahnke W
NMR spectroscopy based discovery and optimization of lead compounds for a given molecular target requires the development of methods with maximum sensitivity and robustness. It is shown here that organic nitroxide radicals ("spin labels") can be used to boost the sensitivity...
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11-24-2010 08:49 PM
The STINT-NMR Method for Studying In-cell Protein-Protein Interactions.
The STINT-NMR Method for Studying In-cell Protein-Protein Interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles The STINT-NMR Method for Studying In-cell Protein-Protein Interactions.
Curr Protoc Protein Sci. 2010 Aug;Chapter 17:Unit17.11
Authors: Burz DS, Shekhtman A
This unit describes critical components and considerations required to study protein-protein structural interactions inside a living cell by using NMR...
Using Singular Value Decomposition to Characterize Protein-Protein Interactions by In-cell NMR Spectroscopy.
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