Understanding pathogenic single-nucleotide polymorphisms in multidomain proteins – studies of isolated domains are not enough
Article first published online: 16 JAN 2013
© 2012 The Authors Journal compilation © 2012 FEBS
Volume 280, Issue 4, pages 1018–1027, February 2013
How to Cite
Randles, L. G., Dawes, G. J. S., Wensley, B. G., Steward, A., Nickson, A. A. and Clarke, J. (2013), Understanding pathogenic single-nucleotide polymorphisms in multidomain proteins – studies of isolated domains are not enough. FEBS Journal, 280: 1018–1027. doi: 10.1111/febs.12094
- Issue published online: 15 FEB 2013
- Article first published online: 16 JAN 2013
- Accepted manuscript online: 14 DEC 2012 07:51AM EST
- Manuscript Accepted: 10 DEC 2012
- Manuscript Received: 6 NOV 2012
- Wellcome Trust. Grant Numbers: WT064417, WT095195
Doc. S1. Analysis of kinetic data for two-domain spectrin fragments.
Fig. S1. Alignments used to identify suitable mutation sites for this study.
Fig. S2. Model proteins used in this study.
Fig. S3. Equilibrium denaturation curves for all single-domain proteins described in this study.
Fig. S4. The linking helix is conserved in spectrin repeats.
Fig. S5. Chevron plot showing folding and unfolding arms.
Fig. S6. Comparison of the folding of R15 and R16 alone and in R1516.
Fig. S7. Comparison of the folding of R16 and R17 alone and in R1617.
Fig. S8. The mutation E106D does not disrupt inter-domain interactions in R1516.
Fig. S9. The mutation I18V does not disrupt inter-domain interactions in R1617.
Fig. S10. The mutation E105P destroys interactions between the domains.
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.