Reduced native state stability in crowded cellular environment due to protein-protein interactions - Wikidata - awgldk - TriplyDB

Reduced native state stability in crowded cellular environment due to protein-protein interactions

Reduced native state stability in crowded cellular environment due to protein-protein interactions

http://www.wikidata.org/entity/Q30427115

about

Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Biomolecular interactions modulate macromolecular structure and dynamics in atomistic model of a bacterial cytoplasm.Probing protein quinary interactions by in-cell nuclear magnetic resonance spectroscopy Quinary protein structure and the consequences of crowding in living cells: leaving the test-tube behind.Denatured state structural property determines protein stabilization by macromolecular crowding: a thermodynamic and structural approach.Quinary structure modulates protein stability in cells.Are current atomistic force fields accurate enough to study proteins in crowded environments?Residue level quantification of protein stability in living cells.Balanced Protein-Water Interactions Improve Properties of Disordered Proteins and Non-Specific Protein Association Insight of the cytotoxicity of the aggregates of peptides or aberrant proteins: a meta-analysis.The effect of macromolecular crowding on the electrostatic component of barnase-barstar binding: a computational, implicit solvent-based study.Macromolecular crowding induces holo α-lactalbumin aggregation by converting to its apo form The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems The Differential Response of Proteins to Macromolecular Crowding Reconstituting Intracellular Vesicle Fusion Reactions: The Essential Role of Macromolecular Crowding Deciphering protein stability in cells.Competitive interactions of ligands and macromolecular crowders with maltose binding protein.Effects of Macromolecular Crowding on the Conformational Ensembles of Disordered Proteins.Minimal effects of macromolecular crowding on an intrinsically disordered protein: a small-angle neutron scattering study.Recent advances in transferable coarse-grained modeling of proteins.Reaching new levels of realism in modeling biological macromolecules in cellular environments.Simple, yet powerful methodologies for conformational sampling of proteins.Microsecond molecular dynamics simulation of guanidinium chloride induced unfolding of ubiquitin.Information flow and protein dynamics: the interplay between nuclear magnetic resonance spectroscopy and molecular dynamics simulations.Nanoscale Assemblies of Small Molecules Control the Fate of Cells Protein Simulations in Fluids: Coupling the OPEP Coarse-Grained Force Field with Hydrodynamics Protein folding, binding, and droplet formation in cell-like conditions.A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.Onset of disorder and protein aggregation due to oxidation-induced intermolecular disulfide bonds: case study of RRM2 domain from TDP-43.Crowding in Cellular Environments at an Atomistic Level from Computer Simulations.Effects of crowding on the stability of a surface-tethered biopolymer: an experimental study of folding in a highly crowded regime.Fluctuation Flooding Method (FFM) for accelerating conformational transitions of proteins.Excluded-volume effects in living cells.Conformational preferences of DNA in reduced dielectric environments.Slow-Down in Diffusion in Crowded Protein Solutions Correlates with Transient Cluster Formation.Quinary interactions with an unfolded state ensemble.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.Kinetic Insights into the Elongation Reaction of Actin Filaments as a Function of Temperature, Pressure, and Macromolecular Crowding.Ion specificity of macromolecules in crowded environments

P2860

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P2860

Reduced native state stability in crowded cellular environment due to protein-protein interactions

http://www.wikidata.org/entity/Q30427115

description

2013 nî lūn-bûn

@nan

2013 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2013 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2013年の論文

@ja

2013年論文

@yue

2013年論文

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

name

Reduced native state stability ...... o protein-protein interactions

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Reduced native state stability ...... o protein-protein interactions

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type

label

Reduced native state stability ...... o protein-protein interactions

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Reduced native state stability ...... o protein-protein interactions

@en

prefLabel

Reduced native state stability ...... o protein-protein interactions

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Reduced native state stability ...... o protein-protein interactions

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P1433

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P2860

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P1433

Journal of the American Chemical Society

P1476

Reduced native state stability ...... o protein-protein interactions

@en

P2093

Michael Feig

http://www.w3.org/2001/XMLSchema#string

Naoya Tochio

http://www.w3.org/2001/XMLSchema#string

Ryuhei Harada

http://www.w3.org/2001/XMLSchema#string

Takanori Kigawa

http://www.w3.org/2001/XMLSchema#string

P2860

Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences

A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G

All-atom empirical potential for molecular modeling and dynamics studies of proteins

VMD: visual molecular dynamics

Extending the treatment of backbone energetics in protein force fields: limitations of gas-phase quantum mechanics in reproducing protein conformational distributions in molecular dynamics simulations

MMTSB Tool Set: enhanced sampling and multiscale modeling methods for applications in structural biology.

High-resolution x-ray crystal structures of the villin headpiece subdomain, an ultrafast folding protein.

Models of macromolecular crowding effects and the need for quantitative comparisons with experiment.

Inside a living cell.

Effect of modulating unfolded state structure on the folding kinetics of the villin headpiece subdomain

P304

3696-3701

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scholarly article

P356

10.1021/JA3126992

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9

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135

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2013-02-20T00:00:00Z

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23402619

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3601481

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