Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.
about
Backtracking on the folding landscape of the beta-trefoil protein interleukin-1beta?Ultrafast folding of WW domains without structured aromatic clusters in the denatured statePFD: a database for the investigation of protein folding kinetics and stabilityTrimming Down a Protein Structure to Its Bare Foldons: SPATIAL ORGANIZATION OF THE COOPERATIVE UNITSelf-consistent determination of the transition state for protein folding: application to a fibronectin type III domain.Calculation of mutational free energy changes in transition states for protein folding.Non-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model.Mechanism of protein folding.Long-range order in the src SH3 folding transition stateTransition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.Point mutations and sequence variability in proteins: redistributions of preexisting populations.Exploring protein domain organization by recognition of secondary structure packing interfaces.Statistical analyses of protein folding rates from the view of quantum transition.Capillarity-like growth of protein folding nuclei.Comparison of successive transition states for folding reveals alternative early folding pathways of two homologous proteins.Quantitative criteria for native energetic heterogeneity influences in the prediction of protein folding kineticsFold and flexibility: what can proteins' mechanical properties tell us about their folding nucleus?Protein unfolding transitions in an intrinsically unstable annexin domain: molecular dynamics simulation and comparison with nuclear magnetic resonance dataAn enhanced partial order curve comparison algorithm and its application to analyzing protein folding trajectoriesThe N-terminal to C-terminal motif in protein folding and functionPhi values in protein-folding kinetics have energetic and structural components.Determination of the folding transition states of barnase by using PhiI-value-restrained simulations validated by double mutant PhiIJ-values.Three key residues form a critical contact network in a protein folding transition state.Constructing, verifying, and dissecting the folding transition state of chymotrypsin inhibitor 2 with all-atom simulationsExperimental evaluation of topological parameters determining protein-folding rates.Investigation of an anomalously accelerating substitution in the folding of a prototypical two-state protein.Phi-value analysis and the nature of protein-folding transition statesSimulation, experiment, and evolution: understanding nucleation in protein S6 folding.Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.The denatured state dictates the topology of two proteins with almost identical sequence but different native structure and function.An amino acid code for protein foldingConstrained proper sampling of conformations of transition state ensemble of protein folding.Folding properties of cytosine monophosphate kinase from E. coli indicate stabilization through an additional insert in the NMP binding domainIndependent 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 stateTypes and effects of protein variations.Site-specific collapse dynamics guide the formation of the cytochrome c' four-helix bundle.Deciphering the folding kinetics of transmembrane helical proteinsThe folding transition state of protein L is extensive with nonnative interactions (and not small and polarized).BPPred: a Web-based computational tool for predicting biophysical parameters of proteins.Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.
P2860
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P2860
Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
name
Mutational analysis of acylpho ...... tact order in protein folding.
@ast
Mutational analysis of acylpho ...... tact order in protein folding.
@en
type
label
Mutational analysis of acylpho ...... tact order in protein folding.
@ast
Mutational analysis of acylpho ...... tact order in protein folding.
@en
prefLabel
Mutational analysis of acylpho ...... tact order in protein folding.
@ast
Mutational analysis of acylpho ...... tact order in protein folding.
@en
P2093
P50
P356
P1476
Mutational analysis of acylpho ...... ntact order in protein folding
@en
P2093
P304
P356
10.1038/14890
P577
1999-11-01T00:00:00Z