Related ArticlesProtein interaction patterns in different cellular environments are revealed by in-cell NMR.
Sci Rep. 2015;5:14456
Authors: Barbieri L, Luchinat E, Banci L
Abstract
In-cell NMR allows obtaining atomic-level information on biological macromolecules in their physiological environment. Soluble proteins may interact with the cellular environment in different ways: either specifically, with their functional partners, or non-specifically, with other cellular components. Such behaviour often causes the disappearance of the NMR signals. Here we show that by introducing mutations on the human protein profilin 1, used here as a test case, the in-cell NMR signals can be recovered. In human cells both specific and non-specific interactions are present, while in bacterial cells only the effect of non-specific interactions is observed. By comparing the NMR signal recovery pattern in human and bacterial cells, the relative contribution of each type of interaction can be assessed. This strategy allows detecting solution in-cell NMR spectra of soluble proteins without altering their fold, thus extending the applicability of in-cell NMR to a wider range of proteins.
PMID: 26399546 [PubMed - as supplied by publisher]
[NMR paper] NMR studies of protein folding and binding in cells and cell-like environments.
NMR studies of protein folding and binding in cells and cell-like environments.
NMR studies of protein folding and binding in cells and cell-like environments.
Curr Opin Struct Biol. 2014 Dec 2;30C:7-16
Authors: Smith AE, Zhang Z, Pielak GJ, Li C
Abstract
Proteins function in cells where the concentration of macromolecules can exceed 300g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein folding and binding...
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12-06-2014 05:18 PM
NMR studies of protein folding and binding in cells and cell-like environments
NMR studies of protein folding and binding in cells and cell-like environments
Publication date: February 2015
Source:Current Opinion in Structural Biology, Volume 30</br>
Author(s): Austin E Smith , Zeting Zhang , Gary J Pielak , Conggang Li</br>
Proteins function in cells where the concentration of macromolecules can exceed 300g/L. The ways in which this crowded environment affects the physical properties of proteins remain poorly understood. We summarize recent NMR-based studies of protein folding and binding conducted in cells and in vitro under crowded...
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12-04-2014 04:37 AM
[NMR paper] Accidental Interaction between PDZ Domains and Diclofenac Revealed by NMR-Assisted Virtual Screening.
Accidental Interaction between PDZ Domains and Diclofenac Revealed by NMR-Assisted Virtual Screening.
Related Articles Accidental Interaction between PDZ Domains and Diclofenac Revealed by NMR-Assisted Virtual Screening.
Molecules. 2013;18(8):9567-81
Authors: Tenno T, Goda N, Umetsu Y, Ota M, Kinoshita K, Hiroaki H
Abstract
In silico approaches have become indispensable for drug discovery as well as drug repositioning and adverse effect prediction. We have developed the eF-seek program to predict protein-ligand interactions based on...
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08-24-2013 04:53 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
Application of SAIL phenylalanine and tyrosine with alternative isotope-labeling patterns for protein structure determination
Application of SAIL phenylalanine and tyrosine with alternative isotope-labeling patterns for protein structure determination
Abstract The extensive collection of NOE constraint data involving the aromatic ring signals is essential for accurate protein structure determination, although it is often hampered in practice by the pervasive signal overlapping and tight spin couplings for aromatic rings. We have prepared various types of stereo-array isotope labeled phenylalanines (ε- and ζ-SAIL Phe) and tyrosine (ε-SAIL Tyr) to overcome these problems (Torizawa et al. 2005), and proven...
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01-09-2011 12:46 PM
[NMR paper] Correlation of the sweetness of variants of the protein brazzein with patterns of hyd
Correlation of the sweetness of variants of the protein brazzein with patterns of hydrogen bonds detected by NMR spectroscopy.
Related Articles Correlation of the sweetness of variants of the protein brazzein with patterns of hydrogen bonds detected by NMR spectroscopy.
J Biol Chem. 2003 Aug 15;278(33):31331-9
Authors: Assadi-Porter FM, Abildgaard F, Blad H, Markley JL
In sequence-function investigations, approaches are needed for rapidly screening protein variants for possible changes in conformation. Recent NMR methods permit direct...
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11-24-2010 09:01 PM
[NMR paper] Protein-protein interaction revealed by NMR T(2) relaxation experiments: the lipoyl d
Protein-protein interaction revealed by NMR T(2) relaxation experiments: the lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.
Related Articles Protein-protein interaction revealed by NMR T(2) relaxation experiments: the lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus.
J Mol Biol. 2000 Jan 28;295(4):1023-37
Authors: Howard MJ, Chauhan HJ, Domingo GJ, Fuller C, Perham RN
T(2) relaxation experiments in combination with...
Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
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