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

Unique interactions between the chromophore and glutamate 16 lead to far-red emission in a red fluorescent protein.

Protein science : a publication of the Protein Society - 1 Feb 2009

Shu Xiaokun, Wang Lei, Colip Leslie, Kallio Karen, Remington S James

Abstract excerpt

mPlum is a far-red fluorescent protein with emission maximum at approximately 650 nm and was derived by directed evolution from DsRed. Two residues near the chromophore, Glu16 and Ile65, were previously revealed to be indispensable for the far-red emission. Ultrafast time-resolved fluorescence emission studies revealed a time dependent shift in the emission maximum, initially about 625 nm, to about 650 nm over a...

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 Glutamic Acid

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Luminescent Proteins

Share to Protein Conformation

Share to Recombinant Proteins

Share to Spectrometry, Fluorescence

Share to Temperature

Source

Open in PubMed Open full text

Identifiers

PMID: 19165727
DOI: 10.1002/pro.66
PMCID: PMC2708057

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

Unique interactions between the chromophore and glutamate 16 lead to far-red emission in a red fluorescent protein.PMID 19165727Read ↗

Hydrogen bond flexibility correlates with Stokes shift in mPlum variants.Semantic proximity Read ↗

Recovery of red fluorescent protein chromophore maturation deficiency through rational design.Semantic proximity Read ↗

Mutagenesis of mNeptune Red-Shifts Emission Spectrum to 681-685 nm.Semantic proximity Read ↗

Mutants of monomeric red fluorescent protein mRFP1 at residue 66: structure modeling by molecular dynamics and search for correlations with spectral properties.Semantic proximity Read ↗

Structure, Function and Dynamics of mCoral, a pH-Responsive Engineered Variant of the mCherry Fluorescent Protein with Improved Hydrogen Peroxide Tolerance.Semantic proximity Read ↗

Exploring the Effects of Mutagenesis on FusionRed by Using Excited-State QM/MM Dynamics and Classical Force Field Simulations.Semantic proximity Read ↗

Juggling with fluorescent proteins: Spectrum and structural changes of the mCardinal2 variants.Semantic proximity Read ↗

Extended Stokes shift in fluorescent proteins: chromophore-protein interactions in a near-infrared TagRFP675 variant.Semantic proximity Read ↗

Analysis of DsRed Mutants. Space around the fluorophore accelerates fluorescence development.Semantic proximity Read ↗

Generation of longer emission wavelength red fluorescent proteins using computationally designed libraries.Semantic proximity Read ↗

Crystal structure of a new cyan fluorescent protein and its hue-shifted variants.Semantic proximity Read ↗

Variants of green fluorescent protein GFPxm.Semantic proximity Read ↗

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