Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.
about
Comparison of DNA extraction methodologies used for assessing fungal diversity via ITS sequencingResidual structure in unfolded proteinsUrea denatured state ensembles contain extensive secondary structure that is increased in hydrophobic proteinsRelationship between enzyme properties and disease progression in Canavan diseaseExploring early stages of the chemical unfolding of proteins at the proteome scaleConformations of a Metastable SH3 Domain Characterized by smFRET and an Excluded-Volume Polymer ModelNative state dynamics drive the unfolding of the SH3 domain of PI3 kinase at high denaturant concentration.Incorporation of (57)Fe-isotopically enriched in apoferritin: formation and characterization of isotopically enriched Fe nanoparticles for metabolic studies.T7 ejectosome assembly: A story unfolds.Quantitative assessment of protein structural models by comparison of H/D exchange MS data with exchange behavior accurately predicted by DXCOREX.Effects of solvents on the intrinsic propensity of peptide backbone conformations.Energetics of the Escherichia coli DnaT protein trimerization reaction.At very low concentrations known chaotropes act as kosmotropes for the N and B isoforms of human serum albumin.A molten globule intermediate of the von Willebrand factor A1 domain firmly tethers platelets under shear flowToward an atomistic description of the urea-denatured state of proteins.Protein destabilisation in ionic liquids: the role of preferential interactions in denaturation.A hypothesis to reconcile the physical and chemical unfolding of proteins.Trimethylamine N-oxide influence on the backbone of proteins: an oligoglycine model.Solubilization of a membrane protein by combinatorial superchargingUrea facilitates the translocation of single-stranded DNA and RNA through the alpha-hemolysin nanopore.Backbone additivity in the transfer model of protein solvation.Hydration of guanidinium depends on its local environment.Guanidinium can both Cause and Prevent the Hydrophobic Collapse of Biomacromolecules.Volume exclusion and soft interaction effects on protein stability under crowded conditions.An extremely halophilic proteobacterium combines a highly acidic proteome with a low cytoplasmic potassium content.Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturationFolded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external regionPeptide conformational preferences in osmolyte solutions: transfer free energies of decaalanine.Glucose interactions with a model peptide.Quantifying why urea is a protein denaturant, whereas glycine betaine is a protein stabilizerMolecular docking simulations for macromolecularly imprinted polymersProbing the Folding-Unfolding Transition of a Thermophilic Protein, MTH1880Preparation and extraction of insoluble (inclusion-body) proteins from Escherichia coli.The role of ionic interactions in the adherence of the Staphylococcus epidermidis adhesin SdrF to prosthetic materialUse of protein folding reagents.Preferential interactions between small solutes and the protein backbone: a computational analysisHost defense proteins derived from human saliva bind to Staphylococcus aureusQuantifying functional group interactions that determine urea effects on nucleic acid helix formation.Cooperative folding near the downhill limit determined with amino acid resolution by hydrogen exchangeDistinctive solvation patterns make renal osmolytes diverse.
P2860
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P2860
Urea, but not guanidinium, destabilizes proteins by forming hydrogen bonds to the peptide group.
description
2009 nî lūn-bûn
@nan
2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Urea, but not guanidinium, des ...... en bonds to the peptide group.
@ast
Urea, but not guanidinium, des ...... en bonds to the peptide group.
@en
type
label
Urea, but not guanidinium, des ...... en bonds to the peptide group.
@ast
Urea, but not guanidinium, des ...... en bonds to the peptide group.
@en
prefLabel
Urea, but not guanidinium, des ...... en bonds to the peptide group.
@ast
Urea, but not guanidinium, des ...... en bonds to the peptide group.
@en
P2093
P2860
P356
P1476
Urea, but not guanidinium, des ...... en bonds to the peptide group.
@en
P2093
Jörg Rösgen
S Walter Englander
Woon Ki Lim
P2860
P304
P356
10.1073/PNAS.0812588106
P407
P577
2009-02-05T00:00:00Z