Macromolecular crowding increases structural content of folded proteins
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Crowded, cell-like environment induces shape changes in aspherical proteinWhat macromolecular crowding can do to a proteinBeyond the excluded volume effects: mechanistic complexity of the crowded milieuQuinary 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.Favourable influence of hydrophobic surfaces on protein structure in porous organically-modified silica glasses.Residue-level interrogation of macromolecular crowding effects on protein stability.Impact of macromolecular crowding on DNA replication.The extracellular protein VlsE is destabilized inside cellsMacromolecular crowding effects on reactions of TePixD (Tll0078).Macromolecular crowding as a suppressor of human IAPP fibril formation and cytotoxicity.A physics-based approach of coarse-graining the cytoplasm of Escherichia coli (CGCYTO).Calcineurin in a Crowded World.Macromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxinCrowding effects on the small, fast-folding protein lambda6-85.Folding, stability and shape of proteins in crowded environments: experimental and computational approachesCosolutes, Crowding, and Protein Folding Kinetics.Effects of macromolecular crowding agents on protein folding in vitro and in silicoThermal aggregation of hen egg white proteins in the presence of salts.Thermodynamic and structural characterization of an antibody gel.Effects of recombinant protein expression on green fluorescent protein diffusion in Escherichia coli.Macromolecular crowding remodels the energy landscape of a protein by favoring a more compact unfolded state.β-galactosidase stability at high substrate concentrations.Modulation of calmodulin plasticity by the effect of macromolecular crowding.Crowding interactions perturb structure and stability by destabilizing the stable core of the α-subunit of tryptophan synthase.The effect of molecular crowding on the stability of human c-MYC promoter sequence I-motif at neutral pH.
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P2860
Macromolecular crowding increases structural content of folded proteins
description
im Oktober 2007 veröffentlichter wissenschaftlicher Artikel
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wetenschappelijk artikel
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наукова стаття, опублікована в жовтні 2007
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name
Macromolecular crowding increases structural content of folded proteins
@en
Macromolecular crowding increases structural content of folded proteins
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type
label
Macromolecular crowding increases structural content of folded proteins
@en
Macromolecular crowding increases structural content of folded proteins
@nl
prefLabel
Macromolecular crowding increases structural content of folded proteins
@en
Macromolecular crowding increases structural content of folded proteins
@nl
P2860
P921
P1433
P1476
Macromolecular crowding increases structural content of folded proteins
@en
P2093
Loren Stagg
Michael Perham
P2860
P304
P356
10.1016/J.FEBSLET.2007.09.049
P407
P577
2007-10-01T00:00:00Z