Fluorescence nanotomography using resonance energy transfer: Demonstration with a protein-sugar complex

Olaf J. Rolinski; David J.S. Birch; Lydia J. McCartney; John C. Pickup

doi:10.1088/0031-9155/46/9/401

Fluorescence nanotomography using resonance energy transfer: Demonstration with a protein-sugar complex

Olaf J. Rolinski, David J.S. Birch, Lydia J. McCartney, John C. Pickup

Physics

Research output: Contribution to journal › Article

Abstract

A new approach to structural sensing, fluorescence resonance energy transfer nanotomography, which interprets fluorescence decay measurement in terms of site density analysis of molecular distributions, has been applied to a glucose sensor based on competitive binding with malachite green labelled dextran to the sugar binding protein concanavalinA labelled with allophycocyanin. Opportunities for structural sensing in clinical medicine are highlighted.

Original language	English
Pages (from-to)	N221-N226
Journal	Physics in Medicine and Biology
Volume	46
Issue number	2001
DOIs	https://doi.org/10.1088/0031-9155/46/9/401
Publication status	Published - 22 Aug 2001

Keywords

fluorescence nanotomography
resonance energy transfer
protein-sugar complex
nanoscience

Access to Document

10.1088/0031-9155/46/9/401

http://dx.doi.org/10.1088/0031-9155/46/9/401

Cite this

Rolinski, O. J., Birch, D. J. S., McCartney, L. J., & Pickup, J. C. (2001). Fluorescence nanotomography using resonance energy transfer: Demonstration with a protein-sugar complex. Physics in Medicine and Biology, 46(2001), N221-N226. https://doi.org/10.1088/0031-9155/46/9/401

@article{591b93baa9f0445d93e895c379b4e9e4,

title = "Fluorescence nanotomography using resonance energy transfer: Demonstration with a protein-sugar complex",

abstract = "A new approach to structural sensing, fluorescence resonance energy transfer nanotomography, which interprets fluorescence decay measurement in terms of site density analysis of molecular distributions, has been applied to a glucose sensor based on competitive binding with malachite green labelled dextran to the sugar binding protein concanavalinA labelled with allophycocyanin. Opportunities for structural sensing in clinical medicine are highlighted.",

keywords = "fluorescence nanotomography, resonance energy transfer, protein-sugar complex, nanoscience",

author = "Rolinski, {Olaf J.} and Birch, {David J.S.} and McCartney, {Lydia J.} and Pickup, {John C.}",

year = "2001",

month = aug,

day = "22",

doi = "10.1088/0031-9155/46/9/401",

language = "English",

volume = "46",

pages = "N221--N226",

journal = "Physics in Medicine and Biology",

issn = "0031-9155",

number = "2001",

}

TY - JOUR

T1 - Fluorescence nanotomography using resonance energy transfer: Demonstration with a protein-sugar complex

AU - Rolinski, Olaf J.

AU - Birch, David J.S.

AU - McCartney, Lydia J.

AU - Pickup, John C.

PY - 2001/8/22

Y1 - 2001/8/22

N2 - A new approach to structural sensing, fluorescence resonance energy transfer nanotomography, which interprets fluorescence decay measurement in terms of site density analysis of molecular distributions, has been applied to a glucose sensor based on competitive binding with malachite green labelled dextran to the sugar binding protein concanavalinA labelled with allophycocyanin. Opportunities for structural sensing in clinical medicine are highlighted.

AB - A new approach to structural sensing, fluorescence resonance energy transfer nanotomography, which interprets fluorescence decay measurement in terms of site density analysis of molecular distributions, has been applied to a glucose sensor based on competitive binding with malachite green labelled dextran to the sugar binding protein concanavalinA labelled with allophycocyanin. Opportunities for structural sensing in clinical medicine are highlighted.

KW - fluorescence nanotomography

KW - resonance energy transfer

KW - protein-sugar complex

KW - nanoscience

UR - http://dx.doi.org/10.1088/0031-9155/46/9/401

U2 - 10.1088/0031-9155/46/9/401

DO - 10.1088/0031-9155/46/9/401

M3 - Article

VL - 46

SP - N221-N226

JO - Physics in Medicine and Biology

JF - Physics in Medicine and Biology

SN - 0031-9155

IS - 2001

ER -