Contact order revisited: influence of protein size on the folding rate.
about
Diverse metastable structures formed by small oligomers of α-synuclein probed by force spectroscopyThe effect of long-range interactions on the secondary structure formation of proteinsPolymer uncrossing and knotting in protein folding, and their role in minimal folding pathwaysUnfolding simulations reveal the mechanism of extreme unfolding cooperativity in the kinetically stable alpha-lytic proteaseThe Trp-cage: optimizing the stability of a globular miniproteinWhen fast is better: protein folding fundamentals and mechanisms from ultrafast approachesAggregation propensity of the human proteomeThe role of non-native interactions in the folding of knotted proteinsUnderstanding protein folding cooperativity based on topological consideration.Monomer topology defines folding speed of heptamer.Assessing the effect of dynamics on the closed-loop protein-folding hypothesisContour length and refolding rate of a small protein controlled by engineered disulfide bonds.Direct observation of parallel folding pathways revealed using a symmetric repeat protein system.Statistical analyses of protein folding rates from the view of quantum transition.Protein contact order prediction from primary sequences.Evolutionary optimization of protein folding.Folding of a LysM domain: entropy-enthalpy compensation in the transition state of an ideal two-state folder.Capillarity-like growth of protein folding nuclei.General mechanism of two-state protein folding kinetics.A comprehensive database of verified experimental data on protein folding kinetics.Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.Single-molecule dynamics reveals cooperative binding-folding in protein recognitionThe energy landscapes of repeat-containing proteins: topology, cooperativity, and the folding funnels of one-dimensional architectures.Golden triangle for folding rates of globular proteins.Studying the unfolding process of protein G and protein L under physical property space.Coupling between properties of the protein shape and the rate of protein folding.Protein aggregation profile of the bacterial cytosol.SeqRate: sequence-based protein folding type classification and rates predictionCharacterizing the regularity of tetrahedral packing motifs in protein tertiary structure.Early events in the folding of four-helix-bundle heme proteinsCharacterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experimentPredicting protein folding rates using the concept of Chou's pseudo amino acid composition.Folding lambda-repressor at its speed limit.Investigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.The rate of the molecular clock and the cost of gratuitous protein synthesisWhy do protein folding rates correlate with metrics of native topology?In vivo translation rates can substantially delay the cotranslational folding of the Escherichia coli cytosolic proteomeScattered Hammond plots reveal second level of site-specific information in protein folding: phi' (beta++).BCL::Score--knowledge based energy potentials for ranking protein models represented by idealized secondary structure elements.Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.
P2860
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P2860
Contact order revisited: influence of protein size on the folding rate.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
2003年论文
@zh
2003年论文
@zh-cn
name
Contact order revisited: influence of protein size on the folding rate.
@en
Contact order revisited: influence of protein size on the folding rate.
@nl
type
label
Contact order revisited: influence of protein size on the folding rate.
@en
Contact order revisited: influence of protein size on the folding rate.
@nl
prefLabel
Contact order revisited: influence of protein size on the folding rate.
@en
Contact order revisited: influence of protein size on the folding rate.
@nl
P2860
P50
P356
P1433
P1476
Contact order revisited: influence of protein size on the folding rate.
@en
P2093
P2860
P304
P356
10.1110/PS.0302503
P577
2003-09-01T00:00:00Z