Controlling the self-assembly of a filamentous hyperthermophilic chaperone by an engineered capping protein

Timothy A. Whitehead, Adam L. Meadows, Douglas S. Clark

Research output: Research - peer-reviewArticle

  • 7 Citations

Abstract

A study was conducted to control the overall filament length of γ prefoldin (γ PFD) using a capping protein. The design of capping protein was depend on a multiple sequence alignment between the γ PFD. Far-UV circular dichroism (CD) spectroscopy of TERM showed secondary structure and thermostability compared with γ PFD. Native gel electrophoresis was utilized to separate short filaments produced by increasing the TERM concentration. The hexameric Mth PFD and the filament distributions were observed using transmission electron microscopy (TEM). The protein has several attributes and potential advantages for the construction of complex, multi-dimensional and functional protein nanostructures. Results show that γ protein allows to design structure and function into protein nanostructures efficiently.

LanguageEnglish (US)
Pages956-960
Number of pages5
JournalSmall
Volume4
Issue number7
DOIs
StatePublished - Jul 2008
Externally publishedYes

Profile

Self assembly
Proteins
prefoldin
Nanostructures
Circular dichroism spectroscopy
Electrophoresis
Ultraviolet spectroscopy
Gels
Transmission electron microscopy
Sequence Alignment
Circular Dichroism
Transmission Electron Microscopy
Spectrum Analysis

Keywords

  • Chaperones
  • Nanobiotechnology
  • Proteins
  • Self-assembly

ASJC Scopus subject areas

  • Biomaterials
  • Engineering (miscellaneous)
  • Biotechnology
  • Medicine(all)

Cite this

Controlling the self-assembly of a filamentous hyperthermophilic chaperone by an engineered capping protein. / Whitehead, Timothy A.; Meadows, Adam L.; Clark, Douglas S.

In: Small, Vol. 4, No. 7, 07.2008, p. 956-960.

Research output: Research - peer-reviewArticle

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