The University of Southampton
University of Southampton Institutional Repository

Structure–function relationships in fluorescent marker proteins of the green fluorescent protein family

Structure–function relationships in fluorescent marker proteins of the green fluorescent protein family
Structure–function relationships in fluorescent marker proteins of the green fluorescent protein family
GFP-like proteins, originally cloned from marine animals, are genetically encoded fluorescence markers that have become indispensable tools for the life sciences. The search for GFP-like proteins with novel and improved properties is ongoing, driven by the persistent need for advanced and specialized fluorescence labels for cellular imaging. The 3D structures of these proteins are overall similar. However, considerable variations have been found in the covalent structures and the stereochemistry of the chromophore, which govern essential optical properties such as the absorption/emission wavelengths. A detailed understanding of the structure and dynamics of GFP-like proteins greatly aids in the rational engineering of advanced fluorescence marker proteins. In this chapter, we summarize the present knowledge of the structural diversity of GFP-like proteins and discuss how structure and dynamics govern their optical properties.
Chromophore, Fluorescent protein, GFP
978-3-642-23371-5
241-263
Springer
Nienhaus, G. Ulrich
64eb2ac6-4fa9-416c-a066-f096d79307cb
Nienhaus, Karin
b05bb626-b88d-48d8-b0ed-cc1624de52ca
Wiedenmann, Jörg
ad445af2-680f-4927-90b3-589ac9d538f7
Jung, G.
Nienhaus, G. Ulrich
64eb2ac6-4fa9-416c-a066-f096d79307cb
Nienhaus, Karin
b05bb626-b88d-48d8-b0ed-cc1624de52ca
Wiedenmann, Jörg
ad445af2-680f-4927-90b3-589ac9d538f7
Jung, G.

Nienhaus, G. Ulrich, Nienhaus, Karin and Wiedenmann, Jörg (2012) Structure–function relationships in fluorescent marker proteins of the green fluorescent protein family. In, Jung, G. (ed.) Fluorescent Proteins I: From understanding to design. (Springer Series on Fluorescence, 11) Dordrecht, NL. Springer, pp. 241-263. (doi:10.1007/4243_2011_15).

Record type: Book Section

Abstract

GFP-like proteins, originally cloned from marine animals, are genetically encoded fluorescence markers that have become indispensable tools for the life sciences. The search for GFP-like proteins with novel and improved properties is ongoing, driven by the persistent need for advanced and specialized fluorescence labels for cellular imaging. The 3D structures of these proteins are overall similar. However, considerable variations have been found in the covalent structures and the stereochemistry of the chromophore, which govern essential optical properties such as the absorption/emission wavelengths. A detailed understanding of the structure and dynamics of GFP-like proteins greatly aids in the rational engineering of advanced fluorescence marker proteins. In this chapter, we summarize the present knowledge of the structural diversity of GFP-like proteins and discuss how structure and dynamics govern their optical properties.

This record has no associated files available for download.

More information

Published date: 2012
Keywords: Chromophore, Fluorescent protein, GFP
Organisations: Ocean and Earth Science

Identifiers

Local EPrints ID: 377018
URI: http://eprints.soton.ac.uk/id/eprint/377018
ISBN: 978-3-642-23371-5
PURE UUID: 9d203c1b-659b-40a4-b781-136f7bbed436
ORCID for Jörg Wiedenmann: ORCID iD orcid.org/0000-0003-2128-2943

Catalogue record

Date deposited: 13 May 2015 10:19
Last modified: 15 Mar 2024 03:28

Export record

Altmetrics

Contributors

Author: G. Ulrich Nienhaus
Author: Karin Nienhaus
Editor: G. Jung

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of http://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×