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

Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.

Biochemistry and cell biology = Biochimie et biologie cellulaire - 1 Apr 2010

Zarrine-Afsar Arash, Lin Sung Lun, Neudecker Philipp

Abstract excerpt

Understanding how proteins adopt their unique native structures requires a complete structural characterization of the rate-limiting transition state(s) along the folding pathway. By definition, transition states are not significantly populated and are only accessible via folding kinetics studies. In this respect, interpreting the kinetic effects of amino acid substitutions (especially to Ala) via Phi-value...

Read the complete abstract on PubMed

Topics

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

Share to Kinetics
Share to Magnetic Resonance Spectroscopy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Folding

Share to Proteins

Share to src Homology Domains

Source

Identifiers

PMID: 20453926
DOI: 10.1139/o09-153

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.PMID 20453926Read ↗

Phi-value analysis of a three-state protein folding pathway by NMR relaxation dispersion spectroscopy.Semantic proximity Read ↗

Mutational Analysis of Protein Folding Transition States: Phi Values.Semantic proximity Read ↗

Protein folding kinetics beyond the phi value: using multiple amino acid substitutions to investigate the structure of the SH3 domain folding transition state.Semantic proximity Read ↗

Transition-states in protein folding kinetics: the structural interpretation of Phi values.Semantic proximity Read ↗

Phi-value analysis and the nature of protein-folding transition states.Semantic proximity Read ↗

Transition states and the meaning of Phi-values in protein folding kinetics.Semantic proximity Read ↗

Experimental investigation of the frequency and substitution dependence of negative phi-values in two-state proteins.Semantic proximity Read ↗

Hydrophobic core packing in the SH3 domain folding transition state.Semantic proximity Read ↗

Transition-state structure as a unifying basis in protein-folding mechanisms: contact order, chain topology, stability, and the extended nucleus mechanism.Semantic proximity Read ↗

Phi values in protein-folding kinetics have energetic and structural components.Semantic proximity Read ↗

Calculation of mutational free energy changes in transition states for protein folding.Semantic proximity Read ↗

Kinetics, thermodynamics and evolution of non-native interactions in a protein folding nucleus.Semantic proximity Read ↗

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