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McNicholas, T.P.* ; Yum, K.* ; Ahn, J.H.* ; Mu, B.* ; Plettenburg, O.* ; Gooderman, A.* ; Natesan, S.* ; Strano, M.S.*

Structure and function of glucose binding protein-single walled carbon nanotube complexes.

Small 8, 3510-3516 (2012)
DOI
Open Access Green as soon as Postprint is submitted to ZB.
Understanding the structure and function of glucose binding proteins (GBP) complexed with single walled carbon nanotubes (SWNTs) is important for the development of applications including fluorescent sensors and nanostructure particle tracking. Herein, circular dichroism (CD), thermal denaturation, photo-absorption spectroscopy and atomic force microscopy are used to study these nanostructures. The protein retains its glucose-binding activity after complexation and is thermally stable below 36 °C. However, the SWNT lowers the midpoint denaturation temperature (Tm) by 5 °C and 4 °C in the absence and presence of 10 mM glucose, respectively. This data highlights that using techniques such as CD and thermal denaturation may be necessary to fully characterize such protein-nanomaterial nanostructures.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Carbon Nanotubes ; Fluorescence ; Glucose ; Periplasmic-binding Proteins
ISSN (print) / ISBN 1613-6810
e-ISSN 1613-6829
Journal Small
Quellenangaben Volume: 8, Issue: 22, Pages: 3510-3516 Article Number: , Supplement: ,
Publisher Wiley
Reviewing status Peer reviewed
Institute(s) Institute of Medicinal Chemistry (IMC)