A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding
about
Characterization of protein-folding pathways by reduced-space modelingImplementation of a k/k0 Method to Identify Long-Range Structure in Transition States during Conformational Folding/Unfolding of ProteinsTrimeric domain-swapped barnaseThe role of a beta-bulge in the folding of the beta-hairpin structure in ubiquitinNMR and SAXS characterization of the denatured state of the chemotactic protein CheY: implications for protein folding initiationFolding of a dimeric beta-barrel: residual structure in the urea denatured state of the human papillomavirus E2 DNA binding domain.Uncoupled analysis of secondary and tertiary protein structure by circular dichroism and electrospray ionization mass spectrometry.The effect of chirality and steric hindrance on intrinsic backbone conformational propensities: tools for protein designA fast method for predicting amino acid mutations that lead to unfolding.Characterization of residual structure in the thermally denatured state of barnase by simulation and experiment: description of the folding pathwayThe hydrogen exchange core and protein folding.Probing site-specific conformational distributions in protein folding with solid-state NMRDetermination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.What can solid state NMR contribute to our understanding of protein folding?Atomic-level structure characterization of an ultrafast folding mini-protein denatured state.Local structural preferences and dynamics restrictions in the urea-denatured state of SUMO-1: NMR characterization.Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturationInsights into Unfolded Proteins from the Intrinsic ϕ/ψ Propensities of the AAXAA Host-Guest Series.Surface point mutations that significantly alter the structure and stability of a protein's denatured stateThe effects of disulfide bonds on the denatured state of barnaseElectrostatic screening and backbone preferences of amino acid residues in urea-denatured ubiquitin.Protein simulations: the absorption spectrum of barnase point mutantsNative and nonnative conformational preferences in the urea-unfolded state of barstar.Refolding simulations of an isolated fragment of barnase into a native-like beta hairpin: evidence for compactness and hydrogen bonding as concurrent stabilizing factors.Initiation sites of protein folding by NMR analysis.Studies of protein folding and dynamics using single molecule fluorescence spectroscopy.A conformational equilibrium in a protein fragment caused by two consecutive capping boxes: 1H-, 13C-NMR, and mutational analysis.Characterization of the unfolded state of bovine alpha-lactalbumin and comparison with unfolded states of homologous proteins.Structure-cytotoxicity relationships in bovine seminal ribonuclease: new insights from heat and chemical denaturation studies on variants.Comparative effects of alcohols (methanol, glycerol) and polyethylene glycol (PEG-300) on acid denatured state of goat liver cystatin.Under-folded proteins: Conformational ensembles and their roles in protein folding, function, and pathogenesis.Ionic-strength-dependent transition of hen egg-white lysozyme at low pH to a compact state and its aggregation on thermal denaturation.Comparison of the amide proton exchange behavior of the rapidly formed folding intermediate and the native state of an antibody scFv fragment
P2860
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P2860
A comparison of the pH, urea, and temperature-denatured states of barnase by heteronuclear NMR: implications for the initiation of protein folding
description
1995 nî lūn-bûn
@nan
1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
name
A comparison of the pH, urea, ...... initiation of protein folding
@ast
A comparison of the pH, urea, ...... initiation of protein folding
@en
A comparison of the pH, urea, ...... initiation of protein folding
@nl
type
label
A comparison of the pH, urea, ...... initiation of protein folding
@ast
A comparison of the pH, urea, ...... initiation of protein folding
@en
A comparison of the pH, urea, ...... initiation of protein folding
@nl
prefLabel
A comparison of the pH, urea, ...... initiation of protein folding
@ast
A comparison of the pH, urea, ...... initiation of protein folding
@en
A comparison of the pH, urea, ...... initiation of protein folding
@nl
P2093
P356
P1476
A comparison of the pH, urea, ...... initiation of protein folding
@en
P2093
A R Fersht
S M Freund
S Vuilleumier
P304
P356
10.1006/JMBI.1995.0618
P407
P577
1995-11-24T00:00:00Z