The osmophobic effect: natural selection of a thermodynamic force in protein folding.
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The role of hyperosmotic stress in inflammation and diseaseNMR structure of the viral peptide linked to the genome (VPg) of poliovirusOrganic compatible solutes of halotolerant and halophilic microorganismsThe Effects of Lipid Membranes, Crowding and Osmolytes on the Aggregation, and Fibrillation Propensity of Human IAPPCation-pi interactions as determinants for binding of the compatible solutes glycine betaine and proline betaine by the periplasmic ligand-binding protein ProX from Escherichia coliStructure of a rabbit muscle fructose-1,6-bisphosphate aldolase A dimer variantStructure of the Nucleocapsid-Binding Domain from the Mumps Virus Polymerase; an Example of Protein Folding Induced by CrystallizationChemical chaperones improve protein secretion and rescue mutant factor VIII in mice with hemophilia AThe effect of chemical chaperones on the assembly and stability of HIV-1 capsid proteinThe osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state.Protein structure, stability and solubility in water and other solvents.The addition of 2,2,2-trifluoroethanol prevents the aggregation of guanidinium around protein and impairs its denaturation ability: a molecular dynamics simulation study.Restoration of structural stability and ligand binding after removal of the conserved disulfide bond in tear lipocalin.The pH Dependence of Saccharides' Influence on Thermal Denaturation of Two Model Proteins Supports an Excluded Volume Model for Stabilization Generalized to Allow for Intramolecular Electrostatic Interactions.Unfolding and refolding of bovine serum albumin at acid pH: ultrasound and structural studies.Ultrasonic studies of alcohol-induced transconformation in beta-lactoglobulin: the intermediate stateBiophysical characterization of Z(SPA-1)--a phage-display selected binder to protein A.Trimethylamine N-oxide influence on the backbone of proteins: an oligoglycine model.An overview of the importance of conformational flexibility in gene regulation by the transcription factors.Crowding alone cannot account for cosolute effect on amyloid aggregationBackbone additivity in the transfer model of protein solvation.Rescue of glaucoma-causing mutant myocilin thermal stability by chemical chaperones.Analysis of strains lacking known osmolyte accumulation mechanisms reveals contributions of osmolytes and transporters to protection against abiotic stressPredicting the energetics of osmolyte-induced protein folding/unfolding.Structural adaptation of extreme halophilic proteins through decrease of conserved hydrophobic contact surface.Osmolyte-induced folding of an intrinsically disordered protein: folding mechanism in the absence of ligand.Therapeutic approaches to delay the onset of Alzheimer's diseaseProtein stability in mixed solvents: a balance of contact interaction and excluded volumeOsmophobic effect of glycerol on irreversible thermal denaturation of rabbit creatine kinaseCompensating effects of urea and trimethylamine-N-oxide on the heteroassociation of α-chymotrypsin and soybean trypsin inhibitorOsmolyte trimethylamine-N-oxide does not affect the strength of hydrophobic interactions: origin of osmolyte compatibility.The osmolyte TMAO stabilizes native RNA tertiary structures in the absence of Mg2+: evidence for a large barrier to folding from phosphate dehydration.Osmoadaptation in bacteria and archaea: common principles and differences.Stabilization of the predominant disease-causing aldolase variant (A149P) with zwitterionic osmolytesEffect of osmolytes on the binding of EGR1 transcription factor to DNA.Probing the kinetic stabilities of Friedreich's ataxia clinical variants using a solid phase GroEL chaperonin capture platform.Protein denaturants at aqueous-hydrophobic interfaces: self-consistent correlation between induced interfacial fluctuations and denaturant stability at the interface.The core trisaccharide of an N-linked glycoprotein intrinsically accelerates folding and enhances stabilityTesting the ability of non-methylamine osmolytes present in kidney cells to counteract the deleterious effects of urea on structure, stability and function of proteins.Strategies to stabilize compact folding and minimize aggregation of antibody-based fragments
P2860
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P2860
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
description
2001 nî lūn-bûn
@nan
2001 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@ast
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@en
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@nl
type
label
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@ast
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@en
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@nl
prefLabel
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@ast
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@en
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@nl
P356
P1476
The osmophobic effect: natural selection of a thermodynamic force in protein folding.
@en
P2093
P304
P356
10.1006/JMBI.2001.4819
P407
P577
2001-07-01T00:00:00Z