Tych, KM, Hoffmann, T, Batchelor, M et al. (6 more authors) (2015) Life in extreme environments: Single molecule force spectroscopy as a tool to explore proteins from extremophilic organisms. Biochemical Society Transactions, 43 (2). 179 - 185. ISSN 0300-5127
Abstract
Extremophiles are organisms which survive and thrive in extreme environments. The proteins from extremophilic single-celled organisms have received considerable attention as they are structurally stable and functionally active under extreme physical and chemical conditions. In this short article, we provide an introduction to extremophiles, the structural adaptations of proteins from extremophilic organisms and the exploitation of these proteins in industrial applications. We provide a review of recent developments which have utilized single molecule force spectroscopy to mechanically manipulate proteins from extremophilic organisms and the information which has been gained about their stability, flexibility and underlying energy landscapes.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Copyright, Publisher and Additional Information: | (c) The Authors Journal compilation (c) 2015 Biochemical Society. This is an author produced version of a paper published in Biochemical Society Transactions. Uploaded in accordance with the publisher's self-archiving policy. |
Keywords: | energy landscape, extreme environments, hyperthermophile, mechanical unfolding, polyprotein, single molecule |
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds) > Molecular & Nanoscale Physics |
Depositing User: | Symplectic Publications |
Date Deposited: | 23 Oct 2015 13:08 |
Last Modified: | 02 Apr 2016 05:43 |
Published Version: | http://dx.doi.org/10.1042/BST20140274 |
Status: | Published |
Publisher: | Portland Press |
Identification Number: | 10.1042/BST20140274 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:91130 |