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Interatomic potentials and solvation parameters from protein engineering data for buried residuesThe nature of protein folding pathwaysContribution of Thr29 to the thermodynamic stability of goat alpha-lactalbumin as determined by experimental and theoretical approachesStructure of the Nucleocapsid-Binding Domain from the Mumps Virus Polymerase; an Example of Protein Folding Induced by CrystallizationStructural insights into the stability perturbations induced by N-terminal variation in human and goat α-lactalbuminA model of dynamic side-chain--side-chain interactions in the alpha-lactalbumin molten globuleExistence of molten globule state in homocysteine-induced protein covalent modificationsChemical and thermal unfolding of a global staphylococcal virulence regulator with a flexible C-terminal endNonuniform chain collapse during early stages of staphylococcal nuclease folding detected by fluorescence resonance energy transfer and ultrarapid mixing methodsDissection of a beta-barrel motif leads to a functional dimer: the case of the intestinal fatty acid binding protein.Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability.Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods.Characterization of the structure and dynamics of a near-native equilibrium intermediate in the unfolding pathway of an all beta-barrel protein.Identification and characterization of an equilibrium intermediate in the unfolding pathway of an all beta-barrel protein.NMR elucidation of early folding hierarchy in HIV-1 protease.Unfolding studies of the cysteine protease baupain, a papain-like enzyme from leaves of Bauhinia forficata: effect of pH, guanidine hydrochloride and temperature.Molecular dynamics simulations of the native and partially folded states of ubiquitin: influence of methanol cosolvent, pH, and temperature on the protein structure and dynamics.Understanding protein non-folding.Temperature-induced unfolding of epidermal growth factor (EGF): insight from molecular dynamics simulationStructural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques.Reversible aggregation plays a crucial role on the folding landscape of p53 core domain.Folding-unfolding of goat alpha-lactalbumin studied by stopped-flow circular dichroism and molecular dynamics simulations.Construction and characterization of protein libraries composed of secondary structure modules.Combinatorial approaches to novel proteins.Accessibility changes within diphtheria toxin T domain when in the functional molten globule state, as determined using hydrogen/deuterium exchange measurements.The p53 core domain is a molten globule at low pH: functional implications of a partially unfolded structure.Collapse of a long axis: single-molecule Förster resonance energy transfer and serpin equilibrium unfolding.Multiple subsets of side-chain packing in partially folded states of alpha-lactalbumins.Local cooperativity in an amyloidogenic state of human lysozyme observed at atomic resolution.Illuminating the off-pathway nature of the molten globule folding intermediate of an α-β parallel protein.Fluorescence of Alexa fluor dye tracks protein folding.Structural and dynamic characteristics of a partially folded state of ubiquitin revealed by hydrogen exchange mass spectrometry.Can misfolded proteins be beneficial? The HAMLET case.Rotavirus NSP4: Cell type-dependent transport kinetics to the exofacial plasma membrane and release from intact infected cellsIndependent of their localization in protein the hydrophobic amino acid residues have no effect on the molten globule state of apomyoglobin and the disulfide bond on the surface of apomyoglobin stabilizes this intermediate stateInhibitor-induced conformational stabilization and structural alteration of a mip-like peptidyl prolyl cis-trans isomerase and its C-terminal domainHeat shock protein 10 (Hsp10) in immune-related diseases: one coin, two sides.Heterogeneity of equilibrium molten globule state of cytochrome c induced by weak salt denaturants under physiological condition.A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the alpha subunit of tryptophan synthase, a TIM barrel proteinIncreased phospholipase A2 activity with phosphorylation of peroxiredoxin 6 requires a conformational change in the protein.
P2860
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P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Role of the molten globule state in protein folding.
@ast
Role of the molten globule state in protein folding.
@en
type
label
Role of the molten globule state in protein folding.
@ast
Role of the molten globule state in protein folding.
@en
prefLabel
Role of the molten globule state in protein folding.
@ast
Role of the molten globule state in protein folding.
@en
P1476
Role of the molten globule state in protein folding
@en
P2093
K Kuwajima
P304
P356
10.1016/S0065-3233(00)53005-8
P577
2000-01-01T00:00:00Z