Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding.
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Clearing and Labeling Techniques for Large-Scale Biological TissuesClarifying Tissue ClearingFolding and Stabilization of Native-Sequence-Reversed Proteins.The Unfolding MD Simulations of Cyclophilin: Analyzed by Surface Contact Networks and Their Associated MetricsMicrobial Cryptotopes are Prominent Targets of B-cell ImmunityExploring early stages of the chemical unfolding of proteins at the proteome scaleNative state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.Interaction-component analysis of the hydration and urea effects on cytochrome c.Sodium perchlorate effects on the helical stability of a mainly alanine peptide.Induction of a Tier-1-like Phenotype in Diverse Tier-2 Isolates by Agents that Guide HIV-1 Env to Perturbation-sensitive, Non-native States.Effects of solvents on the intrinsic propensity of peptide backbone conformations.Quantitative characterization of local protein solvation to predict solvent effects on protein structure.Toward an atomistic description of the urea-denatured state of proteins.Microscopic insights into the protein-stabilizing effect of trimethylamine N-oxide (TMAO)A hypothesis to reconcile the physical and chemical unfolding of proteins.Properties of the cuticular proteins of Anopheles gambiae as revealed by serial extraction of adults.Dissecting the critical factors for thermodynamic stability of modular proteins using molecular modeling approach.Backbone additivity in the transfer model of protein solvation.Using simulations to provide the framework for experimental protein folding studiesProbing osmolyte participation in the unfolding transition state of a protein.Spherical monovalent ions at aqueous liquid-vapor interfaces: interfacial stability and induced interface fluctuations.The structural basis of urea-induced protein unfolding in β-cateninQuantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturationBackbone and side-chain contributions in protein denaturation by urea.Protein denaturants at aqueous-hydrophobic interfaces: self-consistent correlation between induced interfacial fluctuations and denaturant stability at the interface.Synergy in protein-osmolyte mixtures.Peptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Fast, antigen-saving multiplex immunoassay to determine levels and avidity of mouse serum antibodies to pertussis, diphtheria, and tetanus antigens.Regulation and aggregation of intrinsically disordered peptidesFluctuation theory of molecular association and conformational equilibria.Site-specific hydration dynamics of globular proteins and the role of constrained water in solvent exchange with amphiphilic cosolvents.Implicit treatment of solvent dispersion forces in protein simulations.A hydrophobic spine stabilizes a surface-exposed α-helix according to analysis of the solvent-accessible surface area.Lack of Dependence of the Sizes of the Mesoscopic Protein Clusters on ElectrostaticsUrea-Water Solvation Forces on Prion StructuresSolute's perspective on how trimethylamine oxide, urea, and guanidine hydrochloride affect water's hydrogen bonding abilityMolecular mechanism for the preferential exclusion of TMAO from protein surfaces.Reducing the dimensionality of the protein-folding search problem.Preferential interactions between small solutes and the protein backbone: a computational analysis
P2860
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P2860
Urea denaturation by stronger dispersion interactions with proteins than water implies a 2-stage unfolding.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Urea denaturation by stronger ...... r implies a 2-stage unfolding.
@en
type
label
Urea denaturation by stronger ...... r implies a 2-stage unfolding.
@en
prefLabel
Urea denaturation by stronger ...... r implies a 2-stage unfolding.
@en
P2093
P2860
P356
P1476
Urea denaturation by stronger ...... r implies a 2-stage unfolding.
@en
P2093
D Thirumalai
Ruhong Zhou
P2860
P304
16928-16933
P356
10.1073/PNAS.0808427105
P407
P577
2008-10-28T00:00:00Z