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 protein
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Insights into interferon regulatory factor activation from the crystal structure of dimeric IRF5Environment-dependent long-range structural distortion in a temperature-sensitive point mutantMapping 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.Clusters of isoleucine, leucine, and valine side chains define cores of stability in high-energy states of globular proteins: Sequence determinants of structure and stability.Betaalpha-hairpin clamps brace betaalphabeta modules and can make substantive contributions to the stability of TIM barrel proteins.Microsecond barrier-limited chain collapse observed by time-resolved FRET and SAXS.Modular control of cross-oligomerization: analysis of superstabilized Hsp90 homodimers in vivo.Identification of residual structure in the unfolded state of ribonuclease H1 from the moderately thermophilic Chlorobium tepidum: comparison with thermophilic and mesophilic homologuesAutonomously folding protein fragments reveal differences in the energy landscapes of homologous RNases HThe H2A-H2B dimeric kinetic intermediate is stabilized by widespread hydrophobic burial with few fully native interactions.Minireview: structural insights into early folding events using continuous-flow time-resolved small-angle X-ray scatteringIndole-3-glycerol-phosphate synthase is recognized by a cold-inducible group II chaperonin in Thermococcus kodakarensis.Long-range side-chain-main-chain interactions play crucial roles in stabilizing the (betaalpha)8 barrel motif of the alpha subunit of tryptophan synthase.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.UV-radiation induced disruption of dry-cavities in human γD-crystallin results in decreased stability and faster unfolding.Interplay between drying and stability of a TIM barrel protein: a combined simulation-experimental study.Folding versus aggregation: polypeptide conformations on competing pathwaysMicrosecond acquisition of heterogeneous structure in the folding of a TIM barrel protein.Clusters of branched aliphatic side chains serve as cores of stability in the native state of the HisF TIM barrel protein.Dewetting and hydrophobic interaction in physical and biological systems.Insights from coarse-grained Gō models for protein folding and dynamics.Folding of the RNA recognition motif (RRM) domains of the amyotrophic lateral sclerosis (ALS)-linked protein TDP-43 reveals an intermediate stateDissecting the contributions of β-hairpin tyrosine pairs to the folding and stability of long-lived human γD-crystallins.Folding of proteins with a flavodoxin-like architecture.Topological frustration in beta alpha-repeat proteins: sequence diversity modulates the conserved folding mechanisms of alpha/beta/alpha sandwich proteins.The complex and specific pMHC interactions with diverse HIV-1 TCR clonotypes reveal a structural basis for alterations in CTL function.Effect of dehydration on the aggregation kinetics of two amyloid peptides.The foldon substructure of staphylococcal nucleaseStructural analysis of kinetic folding intermediates for a TIM barrel protein, indole-3-glycerol phosphate synthase, by hydrogen exchange mass spectrometry and Gō model simulation.Non-native structure appears in microseconds during the folding of E. coli RNase H.Kinetically trapped metastable intermediate of a disulfide-deficient mutant of the starch-binding domain of glucoamylase.Evidence of a folding intermediate in RNase H from single-molecule FRET experiments.Comparative analysis of thermal unfolding simulations of RNA recognition motifs (RRMs) of TAR DNA-binding protein 43 (TDP-43).Structural Rearrangement upon Fragmentation of the Stability Core of the ALS-Linked Protein TDP-43.Folding and misfolding in a naturally occurring circularly permuted PDZ domain.Crowding interactions perturb structure and stability by destabilizing the stable core of the α-subunit of tryptophan synthase.Triphenylalanine peptides self-assemble into nanospheres and nanorods that are different from the nanovesicles and nanotubes formed by diphenylalanine peptides.Roles for the two N-terminal (β/α) modules in the folding of a (β/α)₈-barrel protein as studied by fragmentation analysis.Computer design of microfluidic mixers for protein/RNA folding studies.
P2860
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P2860
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 protein
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
A tightly packed hydrophobic c ...... synthase, a TIM barrel protein
@ast
A tightly packed hydrophobic c ...... synthase, a TIM barrel protein
@en
type
label
A tightly packed hydrophobic c ...... synthase, a TIM barrel protein
@ast
A tightly packed hydrophobic c ...... synthase, a TIM barrel protein
@en
prefLabel
A tightly packed hydrophobic c ...... synthase, a TIM barrel protein
@ast
A tightly packed hydrophobic c ...... synthase, a TIM barrel protein
@en
P2093
P2860
P1476
A tightly packed hydrophobic c ...... synthase, a TIM barrel protein
@en
P2093
C Robert Matthews
Ramakrishna Vadrevu
Sagar Kathuria
Xiaoyan Yang
P2860
P304
P356
10.1016/J.JMB.2006.12.005
P407
P577
2006-12-15T00:00:00Z