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

Fundamental link between folding states and functional states of proteins.

Journal of the American Chemical Society - 25 Nov 2009

Kalbitzer Hans Robert, Spoerner Michael, Ganser Petra, Hozsa Constantin, Kremer Werner

Abstract excerpt

Folding and function of proteins are two aspects of proteins which are usually considered as basically unrelated phenomena that are optimized by evolution independently. From the funnel model of folding/unfolding and the associated energy landscape, we infer the paradigm that the minimum number of folding intermediates is determined by the number of all functional states of a protein ("essential" folding...

Read the complete abstract on PubMed

Topics

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

Share to Entropy
Share to Guanine Nucleotide Exchange Factors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Triphosphate

Share to Nuclear Magnetic Resonance, Biomolecular

Share to Protein Conformation

Share to Protein Folding

Share to ras Proteins

Share to Signal Transduction

Source

Identifiers

PMID: 19856908
DOI: 10.1021/ja904314q

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Fundamental link between folding states and functional states of proteins.PMID 19856908Read ↗

Conformational states of ADP ribosylation factor 1 complexed with different guanosine triphosphates as studied by 31P NMR spectroscopy.Semantic proximity Read ↗

Dynamically encoded reactivity of Ras enzymes: opening new frontiers for drug discovery.Semantic proximity Read ↗

A detailed thermodynamic analysis of ras/effector complex interfaces.Semantic proximity Read ↗

Mathematics, thermodynamics, and modeling to address ten common misconceptions about protein structure, folding, and stability.Semantic proximity Read ↗

Protein folding: Vexing debates on a fundamental problem.Semantic proximity Read ↗

Unfolded proteins and protein folding studied by NMR.Semantic proximity Read ↗

The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain.Semantic proximity Read ↗

Demonstration by burst-phase analysis of a robust folding intermediate in the FF domain.Semantic proximity Read ↗

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

Unspecific hydrophobic stabilization of folding transition states.Semantic proximity Read ↗

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

The transition state of the ras binding domain of Raf is structurally polarized based on Phi-values but is energetically diffuse.Semantic proximity Read ↗

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