The osmolyte trimethylamine‐N‐oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state

doi:10.1002/pro.52

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The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state

Sung Lun Lin^1,†,
Arash Zarrine-Afsar^1,†,
Alan R. Davidson^1,2,*

Article first published online: 6 JAN 2009

DOI: 10.1002/pro.52

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Protein Science

Volume 18, Issue 3, pages 526–536, March 2009

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How to Cite

Lin, S. L., Zarrine-Afsar, A. and Davidson, A. R. (2009), The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state. Protein Science, 18: 526–536. doi: 10.1002/pro.52

Author Information

¹
Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada M5S-1A8
²
Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada M5S-1A8

^†
Sung Lun Lin and Arash Zarrine-Afsar contributed equally to this work.

Email: Alan R. Davidson (alan.davidson@utoronto.ca)

^*Department of Molecular Genetics, University of Toronto, Toronto, ON, Canada M5S-1A8

Publication History

Issue published online: 23 FEB 2009
Article first published online: 6 JAN 2009
Accepted manuscript online: 6 JAN 2009 12:00AM EST
Manuscript Accepted: 17 DEC 2008
Manuscript Revised: 15 DEC 2008
Manuscript Received: 31 OCT 2008

Funded by

Canadian Institutes of Health Research. Grant Number: MOP-13609

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The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state

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The osmolyte trimethylamine-N-oxide stabilizes the Fyn SH3 domain without altering the structure of its folding transition state

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