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Structure and Function of Glucose Binding Protein–Single Walled Carbon Nanotube Complexes
Author(s) -
McNicholas Thomas P.,
Yum Kyungsuk,
Ahn JinHo,
Mu Bin,
Plettenburg Oliver,
Gooderman Annlouise,
Natesan Sridaran,
Strano Michael S.
Publication year - 2012
Publication title -
small
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.785
H-Index - 236
eISSN - 1613-6829
pISSN - 1613-6810
DOI - 10.1002/smll.201200649
Subject(s) - carbon nanotube , circular dichroism , denaturation (fissile materials) , nanomaterials , nanostructure , materials science , nanotechnology , biophysics , crystallography , chemistry , nuclear chemistry , biology
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 (T m ) 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.