Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics.
about
Polymer uncrossing and knotting in protein folding, and their role in minimal folding pathwaysBCL::Fold--de novo prediction of complex and large protein topologies by assembly of secondary structure elementsAn alanine-zipper structure determined by long range intermolecular interactionsStructural features of cytochrome c' folding intermediates revealed by fluorescence energy-transfer kinetics.The Trp-cage: optimizing the stability of a globular miniproteinExamination of the folding of E. coli CspA through tryptophan substitutionsCharacterization of Protein-Protein Interfaces through a Protein Contact Network ApproachA simple model predicts experimental folding rates and a hub-like topologyViral proteins acquired from a host converge to simplified domain architecturesSimilarity and difference in the unfolding of thermophilic and mesophilic cold shock proteins studied by molecular dynamics simulationsThe effects of nonnative interactions on protein folding rates: theory and simulationMonomer topology defines folding speed of heptamer.Early formation of a beta hairpin during folding of staphylococcal nuclease H124L as detected by pulsed hydrogen exchangeOn the polymer physics origins of protein folding thermodynamics.Contact order and ab initio protein structure predictionAssessing the effect of dynamics on the closed-loop protein-folding hypothesisContour length and refolding rate of a small protein controlled by engineered disulfide bonds.How the folding rates of two- and multistate proteins depend on the amino acid properties.Reduced alphabet for protein folding prediction.Network measures for protein folding state discriminationBiological synthesis of circular polypeptidesCytochrome c' folding triggered by electron transfer: fast and slow formation of four-helix bundlesProtein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.NMR chemical shift analysis of the conformational transition between the monomer and tetramer of melittin in an aqueous solution.The N-terminal to C-terminal motif in protein folding and functionStructural specificity conferred by a group I RNA peripheral element.Local and long-range stability in tandemly arrayed tetratricopeptide repeatsModulation of frustration in folding by sequence permutation.How the folding rate constant of simple, single-domain proteins depends on the number of native contactsExperimental evaluation of topological parameters determining protein-folding rates.The experimental folding landscape of monomeric lactose repressor, a large two-domain protein, involves two kinetic intermediates.Characterization of the folding landscape of monomeric lactose repressor: quantitative comparison of theory and experimentUniversality classes in folding times of proteins.Insights into nucleic acid conformational dynamics from massively parallel stochastic simulationsInvestigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.Why do protein folding rates correlate with metrics of native topology?Universality in the timescales of internal loop formation in unfolded proteins and single-stranded oligonucleotides.Missense meanderings in sequence space: a biophysical view of protein evolution.ProtDCal: A program to compute general-purpose-numerical descriptors for sequences and 3D-structures of proteins.Surfactant copolymers prevent aggregation of heat denatured lysozyme.
P2860
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P2860
Topology, stability, sequence, and length: defining the determinants of two-state protein folding kinetics.
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին 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
Topology, stability, sequence, ...... tate protein folding kinetics.
@ast
Topology, stability, sequence, ...... tate protein folding kinetics.
@en
Topology, stability, sequence, ...... tate protein folding kinetics.
@nl
type
label
Topology, stability, sequence, ...... tate protein folding kinetics.
@ast
Topology, stability, sequence, ...... tate protein folding kinetics.
@en
Topology, stability, sequence, ...... tate protein folding kinetics.
@nl
prefLabel
Topology, stability, sequence, ...... tate protein folding kinetics.
@ast
Topology, stability, sequence, ...... tate protein folding kinetics.
@en
Topology, stability, sequence, ...... tate protein folding kinetics.
@nl
P2093
P356
P1433
P1476
Topology, stability, sequence, ...... tate protein folding kinetics.
@en
P2093
P304
11177-11183
P356
10.1021/BI000200N
P407
P577
2000-09-01T00:00:00Z