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

Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein.

The journal of physical chemistry letters - 16 Jan 2020

Shibazaki Chie, Shimizu Rumi, Kagotani Yuji, Ostermann Andreas, Schrader Tobias E, Adachi Motoyasu

Abstract excerpt

Neutron crystallography has been used to elucidate the protonation states for the enhanced green fluorescent protein, which has revolutionized imaging technologies. The structure has a deprotonated hydroxyl group in the fluorescent chromophore. Also, the protonation states of His148 and Thr203, as well as the orientation of a critical water molecule in direct contact with the chromophore, could be determined. The...

Read the complete abstract on PubMed

Topics

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

Share to Crystallography, X-Ray
Share to Green Fluorescent Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutant Proteins

Share to Mutation

Share to Protons

Share to Static Electricity

Source

Identifiers

PMID: 31880458
DOI: 10.1021/acs.jpclett.9b03252

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

Direct Observation of the Protonation States in the Mutant Green Fluorescent Protein.PMID 31880458Read ↗

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

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

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

pH-dependent transient conformational states control optical properties in cyan fluorescent protein.Semantic proximity Read ↗

Proton pathways in green fluorescence protein.Semantic proximity Read ↗

A strategic fluorescence labeling of D-galactose/D-glucose-binding protein from Escherichia coli helps to shed light on the protein structural stability and dynamics.Semantic proximity Read ↗

Crystallographic and energetic analysis of binding of selected anions to the yellow variants of green fluorescent protein.Semantic proximity Read ↗

A specific interdomain interaction preserves the structural and binding properties of the ModA protein from the phytopathogen Xanthomonas citri domain interaction and transport in ModA.Semantic proximity Read ↗

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

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

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

Exploring the functional residues in a flavin-binding fluorescent protein using deep mutational scanning.Semantic proximity Read ↗

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