Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
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Restoration of structural stability and ligand binding after removal of the conserved disulfide bond in tear lipocalin.How osmolytes influence hydrophobic polymer conformations: A unified view from experiment and theory.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)When does trimethylamine N-oxide fold a polymer chain and urea unfold it?Multisite ion model in concentrated solutions of divalent cations (MgCl2 and CaCl2): osmotic pressure calculations.Regulation and aggregation of intrinsically disordered peptidesSolvation free energy of the peptide group: its model dependence and implications for the additive-transfer free-energy model of protein stabilityDistinctive solvation patterns make renal osmolytes diverse.Trimethylamine-N-Oxide Treatment Induces Changes in the ATP-Binding Cassette Transporter A1 and Scavenger Receptor A1 in Murine Macrophage J774A.1 cells.Thermodynamics of Hydrophobic Amino Acids in Solution: A Combined Experimental-Computational Study.Trimethylamine-N-oxide: its hydration structure, surface activity, and biological function, viewed by vibrational spectroscopy and molecular dynamics simulations.Design principles for high-pressure force fields: Aqueous TMAO solutions from ambient to kilobar pressures.Are stabilizing osmolytes preferentially excluded from the protein surface? FTIR and MD studies.Trimethylamine N-oxide stabilizes proteins via a distinct mechanism compared with betaine and glycine.Influence of TMAO and urea on the structure of water studied by inelastic X-ray scattering.TMAO mediates effective attraction between lipid membranes by partitioning unevenly between bulk and lipid domains.Crowders and Cosolvents-Major Contributors to the Cellular Milieu and Efficient Means to Counteract Environmental Stresses.Can an ammonium-based room temperature ionic liquid counteract the urea-induced denaturation of a small peptide?Modulation of the Polymerization Kinetics of α/β-Tubulin by Osmolytes and Macromolecular Crowding.TMAO and urea in the hydration shell of the protein SNase.Effects of Trimethylamine-N-oxide on the Conformation of Peptides and its Implications for Proteins.A chemical chaperone induces inhomogeneous conformational changes in flexible proteins.Toward Extreme Biophysics: Deciphering the Infrared Response of Biomolecular Solutions at High Pressures.A new force field including charge directionality for TMAO in aqueous solution
P2860
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P2860
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
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2012年论文
@zh-cn
name
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
@ast
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
@en
type
label
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
@ast
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
@en
prefLabel
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
@ast
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
@en
P2093
P2860
P356
P1476
Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.
@en
P2093
Angel E Garcia
Deepak R Canchi
Donald C Rau
George I Makhatadze
Pruthvi Jayasimha
P2860
P304
12095-12104
P356
10.1021/JP304298C
P407
P577
2012-10-01T00:00:00Z