Evidence map›Paper›PMID 15210939›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2004

A fluorescence resonance energy transfer-derived structure of a quantum dot-protein bioconjugate nanoassembly.

I L Medintz, J H Konnert, A R Clapp, I Stanish, M E Twigg, H Mattoussi, J M Mauro, J R Deschamps

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
15.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

37 citing papers in PubMed, 277 citations in OpenAlex.

  1. Article
  2. Design and synthesis of a small molecular NIR-II chemiluminescence probe for in vivoProceedings of the National Academy of Sciences of the United States of America · 2023
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  13. QD-Based FRET Probes at a Glance.Sensors (Basel, Switzerland) · 2015
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 1 country.

I L MedintzCenter for Bio/Molecular Science and Engineering, Code 6900, U.S. Naval Research Laboratory, Washington, DC 20375, USA. imedintz@cbsme.nrl.navy.mil
J H Konnert
A R Clapp
I Stanish
M E Twigg
H Mattoussi
J M Mauro
J R Deschamps
United States Naval Research Laboratory · USNaval Research Laboratory Center for Bio/Molecular Science and Engineering

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The first generation of luminescent semiconductor quantum dot (QD)-based hybrid inorganic biomaterials and sensors is now being developed. It is crucial to understand how bioreceptors, especially proteins, interact with these inorganic nanomaterials. As a model system for study, we use Rhodamine red-labeled engineered variants of Escherichia coli maltose-binding protein (MBP) coordinated to the surface of 555-nm emitting CdSe-ZnS core-shell QDs. Fluorescence resonance energy transfer studies were performed to determine the distance from each of six unique MBP-Rhodamine red dye-acceptor locations to the center of the energy-donating QD. In a strategy analogous to a nanoscale global positioning system determination, we use the intraassembly distances determined from the fluorescence resonance energy transfer measurements, the MBP crystallographic coordinates, and a least-squares approach to determine the orientation of the MBP relative to the QD surface. Results indicate that MBP has a preferred orientation on the QD surface. The refined model is in agreement with other evidence, which indicates coordination of the protein to the QD occurs by means of its C-terminal pentahistidine tail, and the size of the QD estimated from the model is in good agreement with physical measurements of QD size. The approach detailed here may be useful in determining the orientation of proteins in other hybrid protein-nanoparticle materials. To our knowledge, this is the first structural model of a hybrid luminescent QD-protein receptor assembly elucidated by using spectroscopic measurements in conjunction with crystallographic and other data.

Indexed as

Fluorescence Resonance Energy TransferNanotechnologyCarrier ProteinsCrystallography, X-RayEscherichia coliMaltose-Binding ProteinsModels, MolecularMutationProtein ConformationRhodaminesSemiconductorsCarrier ProteinsMaltose-Binding ProteinsRhodamines

Identifiers

PMID15210939
PMCPMC470723
OpenAlexW1997526812

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.