Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Structural characterization of the transition state for folding of muscle acylphosphatase.

Journal of molecular biology - 6 Nov 1998

Chiti F, Taddei N, van Nuland N A, Magherini F, Stefani M, Ramponi G, Dobson C M

Abstract excerpt

The transition state for folding of a small protein, muscle acylphosphatase, has been studied by measuring the rates of folding and unfolding under a variety of solvent conditions. A strong dependence of the folding rate on the concentration of urea suggests the occurrence in the transition state of a large shielding of those groups that are exposed to interaction with the denaturant in the unfolded state (mainly...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Circular Dichroism
Share to Cysteine
Share to Kinetics

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Muscles

Share to Mutation

Share to Protein Folding

Share to Temperature

Share to Thermodynamics

Source

Identifiers

PMID: 9790847
DOI: 10.1006/jmbi.1998.2010

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural characterization of the transition state for folding of muscle acylphosphatase.PMID 9790847Read ↗

Mutational analysis of acylphosphatase suggests the importance of topology and contact order in protein folding.Semantic proximity Read ↗

Stabilisation of alpha-helices by site-directed mutagenesis reveals the importance of secondary structure in the transition state for acylphosphatase folding.Semantic proximity Read ↗

Folding and aggregation are selectively influenced by the conformational preferences of the alpha-helices of muscle acylphosphatase.Semantic proximity Read ↗

Three key residues form a critical contact network in a protein folding transition state.Semantic proximity Read ↗

Structural and thermodynamic investigations on the aggregation and folding of acylphosphatase by molecular dynamics simulations and solvation free energy analysis.Semantic proximity Read ↗

Electrostatic interactions in the denatured state and in the transition state for protein folding: effects of denatured state interactions on the analysis of transition state structure.Semantic proximity Read ↗

Mutational analysis of the aggregation-prone and disaggregation-prone regions of acylphosphatase.Semantic proximity Read ↗

Biological function in a non-native partially folded state of a protein.Semantic proximity Read ↗

Understanding the Binding Induced Folding of Intrinsically Disordered Proteins by Protein Engineering: Caveats and Pitfalls.Semantic proximity Read ↗

Urea-Dependent Adenylate Kinase Activation following Redistribution of Structural States.Semantic proximity Read ↗

Ligand Entry into Fatty Acid Binding Protein via Local Unfolding instead of Gap WideningSemantic proximity Read ↗

Insights into steroidogenic acute regulatory protein (StAR)-dependent cholesterol transfer in mitochondria: evidence from molecular modeling and structure-based thermodynamics supporting the existence of partially unfolded states of StAR.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.