A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway

Travis Clarke Beddoe; Simon Robert Bushell; Matthew A Perugini; Trevor Lithgow; Terrence D Mulhern; Stephen Paul Bottomley; Jamie Rossjohn

doi:10.1074/jbc.M405639200

A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway

Travis Clarke Beddoe, Simon Robert Bushell, Matthew A Perugini, Trevor Lithgow, Terrence D Mulhern, Stephen Paul Bottomley, Jamie Rossjohn

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › Research › peer-review

23 Citations (Scopus)

Original language	English
Pages (from-to)	46448 - 46454
Number of pages	7
Journal	Journal of Biological Chemistry
Volume	279
Issue number	45
DOIs	https://doi.org/10.1074/jbc.M405639200
Publication status	Published - 2004

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Beddoe, T. C., Bushell, S. R., Perugini, M. A., Lithgow, T., Mulhern, T. D., Bottomley, S. P., & Rossjohn, J. (2004). A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway. Journal of Biological Chemistry, 279(45), 46448 - 46454. https://doi.org/10.1074/jbc.M405639200

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author = "Beddoe, \{Travis Clarke\} and Bushell, \{Simon Robert\} and Perugini, \{Matthew A\} and Trevor Lithgow and Mulhern, \{Terrence D\} and Bottomley, \{Stephen Paul\} and Jamie Rossjohn",

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Beddoe, TC, Bushell, SR, Perugini, MA, Lithgow, T, Mulhern, TD, Bottomley, SP & Rossjohn, J 2004, 'A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway', Journal of Biological Chemistry, vol. 279, no. 45, pp. 46448 - 46454. https://doi.org/10.1074/jbc.M405639200

A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway. / Beddoe, Travis Clarke; Bushell, Simon Robert; Perugini, Matthew A et al.
In: Journal of Biological Chemistry, Vol. 279, No. 45, 2004, p. 46448 - 46454.

Research output: Contribution to journal › Article › Research › peer-review

TY - JOUR

T1 - A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway

AU - Beddoe, Travis Clarke

AU - Bushell, Simon Robert

AU - Perugini, Matthew A

AU - Lithgow, Trevor

AU - Mulhern, Terrence D

AU - Bottomley, Stephen Paul

AU - Rossjohn, Jamie

PY - 2004

Y1 - 2004

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DO - 10.1074/jbc.M405639200

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VL - 279

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EP - 46454

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

IS - 45

ER -

Beddoe TC, Bushell SR, Perugini MA, Lithgow T, Mulhern TD, Bottomley SP et al. A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway. Journal of Biological Chemistry. 2004;279(45):46448 - 46454. doi: 10.1074/jbc.M405639200

A biophysical analysis of the tetratricopeptide repeat-rich mitochondrial import receptor, Tom70, reveals an elongated monomer that is inherently flexible, unstable, and unfolds via a multistate pathway

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