A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation.
about
Protein domain definition should allow for conditional disorderThermodynamics of interactions of urea and guanidinium salts with protein surface: relationship between solute effects on protein processes and changes in water-accessible surface areaThe influence of chemical chaperones on enzymatic activity under thermal and chemical stresses: common features and variation among diverse chemical familiesEntropic stabilization of proteins by TMAOReconstitution of the trimethylamine oxide reductase regulatory elements of Shewanella oneidensis in Escherichia coli.The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.Amyloid-like fibril formation in an all beta-barrel protein involves the formation of partially structured intermediate(s).A comparison of experimental and computational methods for mapping the interactions present in the transition state for folding of FKBP12The addition of 2,2,2-trifluoroethanol prevents the aggregation of guanidinium around protein and impairs its denaturation ability: a molecular dynamics simulation study.Osmotically induced helix-coil transition in poly(glutamic acid).Salt potentiates methylamine counteraction system to offset the deleterious effects of urea on protein stability and function.How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory.Interaction-component analysis of the hydration and urea effects on cytochrome c.Molecular Effects of Concentrated Solutes on Protein Hydration, Dynamics, and Electrostatics.Evolutionary bridges to new protein folds: design of C-terminal Cro protein chameleon sequences.Trimethylamine-N-oxide counteracts urea effects on rabbit muscle lactate dehydrogenase function: a test of the counteraction hypothesis.Microscopic stability of cold shock protein A examined by NMR native state hydrogen exchange as a function of urea and trimethylamine N-oxideTorC apocytochrome negatively autoregulates the trimethylamine N-oxide (TMAO) reductase operon in Escherichia coli.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)A hypothesis to reconcile the physical and chemical unfolding of proteins.Using a second-order differential model to fit data without baselines in protein isothermal chemical denaturationTorT, a member of a new periplasmic binding protein family, triggers induction of the Tor respiratory system upon trimethylamine N-oxide electron-acceptor binding in Escherichia coli.Trimethylamine oxide counteracts effects of hydrostatic pressure on proteins of deep-sea teleosts.Identifying protein stabilizing ligands using GroEL.Osmosensing by bacteria: signals and membrane-based sensorsTrimethylamine N-oxide influence on the backbone of proteins: an oligoglycine model.Counteraction of urea-induced protein denaturation by trimethylamine N-oxide: a chemical chaperone at atomic resolution.The hydration structure of guanidinium and thiocyanate ions: implications for protein stability in aqueous solutionConditional mutations in the mitotic chromosome binding function of the bovine papillomavirus type 1 E2 protein.A role for indels in the evolution of Cro protein folds.Effect of osmolytes on protein dynamics in the lactate dehydrogenase-catalyzed reaction.Backbone additivity in the transfer model of protein solvation.Rescue of glaucoma-causing mutant myocilin thermal stability by chemical chaperones.Organic solutes rescue the functional defect in delta F508 cystic fibrosis transmembrane conductance regulator.The TorR high-affinity binding site plays a key role in both torR autoregulation and torCAD operon expression in Escherichia coliPredicting the energetics of osmolyte-induced protein folding/unfolding.Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.Time-dependent effects of trimethylamine-N-oxide/urea on lactate dehydrogenase activity: an unexplored dimension of the adaptation paradigm.Excluded volume in solvation: sensitivity of scaled-particle theory to solvent size and densityMolecular dynamics of solid-state lysozyme as affected by glycerol and water: a neutron scattering study.
P2860
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P2860
A naturally occurring protective system in urea-rich cells: mechanism of osmolyte protection of proteins against urea denaturation.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
A naturally occurring protecti ...... ins against urea denaturation.
@ast
A naturally occurring protecti ...... ins against urea denaturation.
@en
type
label
A naturally occurring protecti ...... ins against urea denaturation.
@ast
A naturally occurring protecti ...... ins against urea denaturation.
@en
prefLabel
A naturally occurring protecti ...... ins against urea denaturation.
@ast
A naturally occurring protecti ...... ins against urea denaturation.
@en
P356
P1433
P1476
A naturally occurring protecti ...... ins against urea denaturation.
@en
P304
P356
10.1021/BI970247H
P407
P577
1997-07-01T00:00:00Z