NMR studies of protein folding and binding in cells and cell-like environments.
about
Challenge of mimicking the influences of the cellular environment on RNA structure by PEG-induced macromolecular crowdingIntrinsic disorder here, there, and everywhere, and nowhere to escape from it.Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy.Physicochemical code for quinary protein interactions in Escherichia coli.Non-Uniform Sampling and J-UNIO Automation for Efficient Protein NMR Structure Determination.The Differential Response of Proteins to Macromolecular CrowdingMacromolecular Crowding In Vitro, In Vivo, and In Between.Protein folding, binding, and droplet formation in cell-like conditions.Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.mRNA cap analogues substituted in the tetraphosphate chain with CX2: identification of O-to-CCl2 as the first bridging modification that confers resistance to decapping without impairing translationIntracellular pH modulates quinary structure.An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states.Protein-protein interaction analysis in crude bacterial lysates using combinational method of 19F site-specific incorporation and 19F NMRSolution structure and interaction with copper in vitro and in living cells of the first BIR domain of XIAP.Stable and rigid DTPA-like paramagnetic tags suitable for in vitro and in situ protein NMR analysis.Interaction proteomics by using in-cell NMR spectroscopy.Crowding interactions perturb structure and stability by destabilizing the stable core of the α-subunit of tryptophan synthase.Surface Charge Modulates Protein-Protein Interactions in Physiologically Relevant Environments.Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy
P2860
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P2860
NMR studies of protein folding and binding in cells and cell-like environments.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
2014年學術文章
@zh
2014年學術文章
@zh-hant
name
NMR studies of protein folding and binding in cells and cell-like environments.
@en
type
label
NMR studies of protein folding and binding in cells and cell-like environments.
@en
prefLabel
NMR studies of protein folding and binding in cells and cell-like environments.
@en
P2093
P1476
NMR studies of protein folding and binding in cells and cell-like environments.
@en
P2093
Austin E Smith
Conggang Li
Gary J Pielak
Zeting Zhang
P356
10.1016/J.SBI.2014.10.004
P577
2014-12-03T00:00:00Z