The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.
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The folding free-energy surface of HIV-1 protease: insights into the thermodynamic basis for resistance to inhibitors.Partial NMR assignments and secondary structure mapping of the isolated alpha subunit of Escherichia coli tryptophan synthase, a 29-kD TIM barrel proteinProtein folding and misfolding: mechanism and principles.Mapping the structure of folding cores in TIM barrel proteins by hydrogen exchange mass spectrometry: the roles of motif and sequence for the indole-3-glycerol phosphate synthase from Sulfolobus solfataricus.Tracking Equilibrium and Nonequilibrium Shifts in Data with TREND.Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli.Equilibrium and kinetic folding pathways of a TIM barrel with a funneled energy landscapeLong-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase.The H2A.Z/H2B dimer is unstable compared to the dimer containing the major H2A isoform.Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome.NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein.Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study.Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein.Domain stabilities in protein kinase R (PKR): evidence for weak interdomain interactionsSpontaneous Unfolding-Refolding of Fibronectin Type III Domains Assayed by Thiol Exchange: THERMODYNAMIC STABILITY CORRELATES WITH RATES OF UNFOLDING RATHER THAN FOLDING.Rat liver betaine-homocysteine S-methyltransferase equilibrium unfolding: insights into intermediate structure through tryptophan substitutions.Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.Unfolding studies on soybean agglutinin and concanavalin a tetramers: a comparative account.Lethal mutations in the major homology region and their suppressors act by modulating the dimerization of the rous sarcoma virus capsid protein C-terminal domain.Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme.Partially unfolded forms and non-two-state folding of a beta-sandwich: FHA domain from Arabidopsis receptor kinase-associated protein phosphatase.Analysis of monomeric and dimeric phosphorylated forms of protein kinase R.Folding and unfolding of gammaTIM monomers and dimers.Rational stabilization of complex proteins: a divide and combine approach.Structural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Gō model simulation.Denatured collapsed states in protein folding: example of apomyoglobin.The folding pathway of glycosomal triosephosphate isomerase: structural insights into equilibrium intermediates.Crowding interactions perturb structure and stability by destabilizing the stable core of the α-subunit of tryptophan synthase.
P2860
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P2860
The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli.
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The progressive development of ...... ynthase from Escherichia coli.
@ast
The progressive development of ...... ynthase from Escherichia coli.
@en
type
label
The progressive development of ...... ynthase from Escherichia coli.
@ast
The progressive development of ...... ynthase from Escherichia coli.
@en
prefLabel
The progressive development of ...... ynthase from Escherichia coli.
@ast
The progressive development of ...... ynthase from Escherichia coli.
@en
P2093
P2860
P356
P1433
P1476
The progressive development of ...... ynthase from Escherichia coli.
@en
P2093
C R Matthews
P J Gualfetti
P2860
P304
P356
10.1110/PS.8.8.1623
P577
1999-08-01T00:00:00Z