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

Unveiling how an archetypal fluorescent protein operates: theoretical perspective on the ultrafast excited state dynamics of GFP variant S65T/H148D.

The journal of physical chemistry. B - 12 Feb 2015

Armengol Pau, Gelabert Ricard, Moreno Miquel, Lluch José M

Abstract excerpt

Green fluorescent protein variant S65T/H148D has been reported to host a photocycle involving the photoinduced proton transfer reaction between the chromophore and residue Asp148 under 50 fs and without a measurable kinetic isotope effect, and experimental evidence is suggestive of the existence of a highly delocalized proton between these residues. The blinding speed at which this biological system undergoes...

Read the complete abstract on PubMed

Topics

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

Share to Hydrogen Bonding
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Protein Structure, Secondary

Share to Protons

Share to Quantum Theory

Share to Solvents

Share to Thermodynamics

Source

Identifiers

PMID: 25144880
DOI: 10.1021/jp506113g

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

Unveiling how an archetypal fluorescent protein operates: theoretical perspective on the ultrafast excited state dynamics of GFP variant S65T/H148D.PMID 25144880Read ↗

New insights into the structure-spectrum relationship in S65T/H148D and E222Q/H148D green fluorescent protein mutants: a theoretical assessment.Semantic proximity Read ↗

Ultrafast excited-state dynamics in the green fluorescent protein variant S65T/H148D. 3. Short- and long-time dynamics of the excited-state proton transfer.Semantic proximity Read ↗

An alternate proton acceptor for excited-state proton transfer in green fluorescent protein: rewiring GFP.Semantic proximity Read ↗

Ultrafast action chemistry in slow motion: atomistic description of the excitation and fluorescence processes in an archetypal fluorescent protein.Semantic proximity Read ↗

Uncovering the hidden ground state of green fluorescent protein.Semantic proximity Read ↗

Theoretical Computer-Aided Mutagenic Study on the Triple Green Fluorescent Protein Mutant S65T/H148D/Y145F.Semantic proximity Read ↗

Slow exchange in the chromophore of a green fluorescent protein variant.Semantic proximity Read ↗

Molecular dynamics simulations of enhanced green fluorescent proteins: effects of F64L, S65T and T203Y mutations on the ground-state proton equilibria.Semantic proximity Read ↗

Role of histidine 148 in stability and dynamics of a highly fluorescent GFP variant.Semantic proximity Read ↗

Photoinduced proton transfer inside an engineered green fluorescent protein: a stepwise-concerted-hybrid reaction.Semantic proximity Read ↗

Photophysics of EGFP (E222H) Mutant, with Comparisons to Model Chromophores: Excited State pK's, Progressions, Quenching and Exciton Interaction.Semantic proximity Read ↗

Green and red fluorescent proteins: photo- and thermally induced dynamics probed by site-selective spectroscopy and hole burning.Semantic proximity Read ↗

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