[NMR paper] Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Protein interaction patterns in different cellular environments are revealed by in-cell NMR.
Related Articles Protein 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...
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09-26-2015 05:13 AM
[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
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...