Measuring the stability of partly folded proteins using TMAO.
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Intestinal microbiota metabolism of L-carnitine, a nutrient in red meat, promotes atherosclerosisMixed osmolytes: the degree to which one osmolyte affects the protein stabilizing ability of anotherA backbone-based theory of protein foldingStructure and stability of the ankyrin domain of the Drosophila Notch receptorConformational selection in the molten globule state of the nuclear coactivator binding domain of CBPMannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motionsStabilizing additives added during cell lysis aid in the solubilization of recombinant proteinsThe osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.Restoration of structural stability and ligand binding after removal of the conserved disulfide bond in tear lipocalin.Osmotically induced helix-coil transition in poly(glutamic acid).Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.Solutes modify a conformational transition in a membrane transport protein.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)Using a second-order differential model to fit data without baselines in protein isothermal chemical denaturationA role for indels in the evolution of Cro protein folds.Naturally occurring osmolyte, trehalose induces functional conformation in an intrinsically disordered activation domain of glucocorticoid receptor.Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.Therapeutic approaches to delay the onset of Alzheimer's diseaseConserved thermodynamic contributions of backbone hydrogen bonds in a protein foldEffect of osmolytes on the binding of EGR1 transcription factor to DNA.Forced folding of a disordered protein accesses an alternative folding landscape.Synergy in protein-osmolyte mixtures.Peptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Testing the ability of non-methylamine osmolytes present in kidney cells to counteract the deleterious effects of urea on structure, stability and function of proteins.A molecular mechanism for osmolyte-induced protein stabilityResveratrol Attenuates Trimethylamine-N-Oxide (TMAO)-Induced Atherosclerosis by Regulating TMAO Synthesis and Bile Acid Metabolism via Remodeling of the Gut MicrobiotaAnatomy of energetic changes accompanying urea-induced protein denaturation.Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor.Tau Aggregation Propensity Engrained in Its Solution State.The H2A.Z/H2B dimer is unstable compared to the dimer containing the major H2A isoform.Molecular mechanism for the preferential exclusion of TMAO from protein surfaces.Intracellular organic osmolytes: function and regulation.Single-Molecule Chemo-Mechanical Spectroscopy Provides Structural Identity of Folding Intermediates.Reconciling the solution and X-ray structures of the villin headpiece helical subdomain: molecular dynamics simulations and double mutant cycles reveal a stabilizing cation-pi interaction.An experimentally determined protein folding energy landscape.Glycosides as compatible solutes: biosynthesis and applications.Osmolyte effects on protein stability and solubility: a balancing act between backbone and side-chains.TMAO-Protein Preferential Interaction Profile Determines TMAO's Conditional In Vivo Compatibility.Are stabilizing osmolytes preferentially excluded from the protein surface? FTIR and MD studies.Protein phase diagrams II: nonideal behavior of biochemical reactions in the presence of osmolytes
P2860
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P2860
Measuring the stability of partly folded proteins using TMAO.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Measuring the stability of partly folded proteins using TMAO.
@ast
Measuring the stability of partly folded proteins using TMAO.
@en
type
label
Measuring the stability of partly folded proteins using TMAO.
@ast
Measuring the stability of partly folded proteins using TMAO.
@en
prefLabel
Measuring the stability of partly folded proteins using TMAO.
@ast
Measuring the stability of partly folded proteins using TMAO.
@en
P2860
P356
P1433
P1476
Measuring the stability of partly folded proteins using TMAO.
@en
P2093
Cecilia C Mello
P2860
P304
P356
10.1110/PS.0372903
P50
P577
2003-07-01T00:00:00Z