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Conformational changes of photoactive yellow protein monitored by terahertz spectroscopy

Abstract:

Observing the structural dynamics of proteins under conditions as close as possible to those in a living organism is essential for understanding the biological functions of proteins accurately. Here we demonstrate that terahertz spectroscopy is a convenient probe of conformational changes in proteins suspended in physiological buffer solution. We have observed that the partial unfolding of photoactive yellow protein leads to a clear increase in absorption at terahertz frequencies. Using norma...

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Publication status:
Published

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Authors


Castro-Camus, E More by this author
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Institution:
University of Oxford
Department:
Oxford, MPLS, Physics, Condensed Matter Physics
Journal:
CHEMICAL PHYSICS LETTERS
Volume:
455
Issue:
4-6
Pages:
289-292
Publication date:
2008-04-10
DOI:
ISSN:
0009-2614
URN:
uuid:6ab41bda-5893-46c8-9900-1abd33657e41
Source identifiers:
5324
Local pid:
pubs:5324
Language:
English

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