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Protein Science (2004), 13:1088-1099. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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The response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinase

Anthony Mittermaier1 and Lewis E. Kay1,2

1 Department of Biochemistry and
2 Departments of Medical Genetics and Chemistry, University of Toronto, Toronto, Ontario, Canada M5S 1A8

(RECEIVED October 31, 2003; FINAL REVISION December 24, 2003; ACCEPTED December 29, 2003)



Abstract

We have used 15N- and 2H-NMR spin relaxation experiments to study the response of backbone and side-chain dynamics when a leucine or valine is substituted for a completely buried phenylalanine residue in the SH3 domain from the Fyn tyrosine kinase. Several residues show differences in the time scales and temperature dependences of internal motions when data for the three proteins are compared. Changes were also observed in the magnitude of dynamics, with the valine, and to a lesser extent leucine mutant, showing enhanced flexibility compared to the wild-type (WT) protein. The motions of many of the same amide and methyl groups are affected by both mutations, identifying a set of loci where dynamics are sensitive to interactions involving the targeted side chain. These results show that contacts within the hydrophobic core affect many aspects of internal mobility throughout the Fyn SH3 domain.

Keywords: NMR relaxation; hydrophobic core; site-directed mutagenesis; protein dynamics

Reprint requests to: Anthony Mittermaier or Lewis E. Kay, Departments of Biochemistry, Chemistry and Medical Genetics, University of Toronto, Toronto, Ontario, Canada M5S 1A8; e-mail: tmitter{at}pound.med.utoronto.ca or kay{at}pound.med.utoronto.ca; fax: (416) 978-6885.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.03502504.


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